‘Renovation of old drugs’ – can peptide drug conjugates lead the post-ADC era?
Chaowei Hao
A B , Peng Chen A B , Hui Zhang A B , Sarra Setrerrahmane C and Hanmei Xu A B *
+ Author Affiliations
- Author Affiliations
A The Engineering Research Center of Synthetic Peptide Drug Discovery and Evaluation of Jiangsu Province, China Pharmaceutical University, Nanjing 210009, China.
B State Key Laboratory of Natural Medicines, Ministry of Education, China Pharmaceutical University, Nanjing 210009, China.
C Nanjing Anji Biotechnology Co. Ltd, Nanjing 210033, China.
Australian Journal of Chemistry 76(8) 318-336 https://doi.org/10.1071/CH22252
Submitted: 2 December 2022 Accepted: 19 January 2023 Published: 30 June 2023
© 2023 The Author(s) (or their employer(s)). Published by CSIRO Publishing.
Abstract
Peptide–drug conjugates (PDCs) are an emerging targeted therapeutic drug following on from the relative success of antibody–drug conjugates (ADCs). In this class, peptides are used to target payload molecules at the disease sites, thereby reducing toxicity and improving the physicochemical properties of the payload. A PDC is composed of three parts: peptide, linker and toxin molecule, and in this structure, the selection of the target in addition to the affinity and stability of the peptide are the keys to the success of PDCs. Since the development of ADCs, drugs have undergone several updates – can PDCs leverage the experience and lessons learned from the development of ADCs over the years to achieve new success? This review presents a systematic introduction of each component of PDCs, as well as the characteristics of PDCs under investigation, with the prospect of PDC development to deepen understanding of their mechanism of action.
Keywords: antibody, cancer, linker, payload, peptide, peptide conjugate, target, toxicity.
References
[1] GR Dagenais, DP Leong, S Rangarajan, F Lanas, P Lopez-Jaramillo, R Gupta, R Diaz, A Avezum, GBF Oliveira, A Wielgosz, SR Parambath, P Mony, KF Alhabib, A Temizhan, N Ismail, J Chifamba, K Yeates, R Khatib, O Rahman, K Zatonska, K Kazmi, L Wei, J Zhu, A Rosengren, K Vijayakumar, M Kaur, V Mohan, A Yusufali, R Kelishadi, KK Teo, P Joseph, S Yusuf, Variations in common diseases, hospital admissions, and deaths in middle-aged adults in 21 countries from five continents (PURE): a prospective cohort study. Lancet 2020, 395, 785.| Variations in common diseases, hospital admissions, and deaths in middle-aged adults in 21 countries from five continents (PURE): a prospective cohort study.Crossref | GoogleScholarGoogle Scholar |
[2] H Sung, J Ferlay, RL Siegel, M Laversanne, I Soerjomataram, A Jemal, F Bray, Global cancer statistics 2020: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries. CA Cancer J Clin 2021, 71, 209.
| Global cancer statistics 2020: GLOBOCAN estimates of incidence and mortality worldwide for 36 cancers in 185 countries.Crossref | GoogleScholarGoogle Scholar |
[3] VT Devita Jr, E Chu, A history of cancer chemotherapy. Cancer Res 2008, 68, 8643.
| A history of cancer chemotherapy.Crossref | GoogleScholarGoogle Scholar |
[4] Z Fu, S Li, S Han, C Shi, Y Zhang, Antibody drug conjugate: the “biological missile” for targeted cancer therapy. Signal Transduct Target Ther 2022, 7, 93.
| Antibody drug conjugate: the “biological missile” for targeted cancer therapy.Crossref | GoogleScholarGoogle Scholar |
[5] S Panowski, S Bhakta, H Raab, P Polakis, JR Junutula, Site-specific antibody drug conjugates for cancer therapy. MAbs 2014, 6, 34.
| Site-specific antibody drug conjugates for cancer therapy.Crossref | GoogleScholarGoogle Scholar |
[6] K Strebhardt, A Ullrich, Paul Ehrlich’s magic bullet concept: 100 years of progress. Nat Rev Cancer 2008, 8, 473.
| Paul Ehrlich’s magic bullet concept: 100 years of progress.Crossref | GoogleScholarGoogle Scholar |
[7] K Tamura, J Tsurutani, S Takahashi, H Iwata, IE Krop, C Redfern, Y Sagara, T Doi, H Park, RK Murthy, RA Redman, T Jikoh, C Lee, M Sugihara, J Shahidi, A Yver, S Modi, Trastuzumab deruxtecan (DS-8201a) in patients with advanced HER2-positive breast cancer previously treated with trastuzumab emtansine: a dose-expansion, phase 1 study. Lancet Oncol 2019, 20, 816.
| Trastuzumab deruxtecan (DS-8201a) in patients with advanced HER2-positive breast cancer previously treated with trastuzumab emtansine: a dose-expansion, phase 1 study.Crossref | GoogleScholarGoogle Scholar |
[8] Y Pommier, Topoisomerase I inhibitors: camptothecins and beyond. Nat Rev Cancer 2006, 6, 789.
| Topoisomerase I inhibitors: camptothecins and beyond.Crossref | GoogleScholarGoogle Scholar |
[9] Y Ogitani, T Aida, K Hagihara, J Yamaguchi, C Ishii, N Harada, M Soma, H Okamoto, M Oitate, S Arakawa, T Hirai, R Atsumi, T Nakada, I Hayakawa, Y Abe, T Agatsuma, DS-8201a, a novel HER2-targeting ADC with a novel DNA topoisomerase I inhibitor, demonstrates a promising antitumor efficacy with differentiation from T-DM1. Clin Cancer Res 2016, 22, 5097.
| DS-8201a, a novel HER2-targeting ADC with a novel DNA topoisomerase I inhibitor, demonstrates a promising antitumor efficacy with differentiation from T-DM1.Crossref | GoogleScholarGoogle Scholar |
[10] Y Ogitani, K Hagihara, M Oitate, H Naito, T Agatsuma, Bystander killing effect of DS-8201a, a novel anti-human epidermal growth factor receptor 2 antibody–drug conjugate, in tumors with human epidermal growth factor receptor 2 heterogeneity. Cancer Sci 2016, 107, 1039.
| Bystander killing effect of DS-8201a, a novel anti-human epidermal growth factor receptor 2 antibody–drug conjugate, in tumors with human epidermal growth factor receptor 2 heterogeneity.Crossref | GoogleScholarGoogle Scholar |
[11] H Wang, Y Sun, X Zhou, C Chen, L Jiao, W Li, S Gou, Y Li, J Du, G Chen, W Zhai, Y Wu, Y Qi, Y Gao, CD47/SIRPα blocking peptide identification and synergistic effect with irradiation for cancer immunotherapy. J Immunother Cancer 2020, 8, e000905.
| CD47/SIRPα blocking peptide identification and synergistic effect with irradiation for cancer immunotherapy.Crossref | GoogleScholarGoogle Scholar |
[12] MA Firer, G Gellerman, Targeted drug delivery for cancer therapy: the other side of antibodies. J Hematol Oncol 2012, 5, 70.
| Targeted drug delivery for cancer therapy: the other side of antibodies.Crossref | GoogleScholarGoogle Scholar |
[13] GP Smith, VA Petrenko, Phage display. Chem Rev 1997, 97, 391.
| Phage display.Crossref | GoogleScholarGoogle Scholar |
[14] L Ma, C Wang, Z He, B Cheng, L Zheng, K Huang, Peptide-drug conjugate: a novel drug design approach. Curr Med Chem 2017, 24, 3373.
| Peptide-drug conjugate: a novel drug design approach.Crossref | GoogleScholarGoogle Scholar |
[15] R Santos, O Ursu, A Gaulton, AP Bento, RS Donadi, CG Bologa, A Karlsson, B Al-Lazikani, A Hersey, TI Oprea, JP Overington, A comprehensive map of molecular drug targets. Nat Rev Drug Discov 2017, 16, 19.
| A comprehensive map of molecular drug targets.Crossref | GoogleScholarGoogle Scholar |
[16] PL Bedard, DM Hyman, MS Davids, LL Siu, Small molecules, big impact: 20 years of targeted therapy in oncology. Lancet 2020, 395, 1078.
| Small molecules, big impact: 20 years of targeted therapy in oncology.Crossref | GoogleScholarGoogle Scholar |
[17] A Zhao, MR Tohidkia, DL Siegel, G Coukos, Y Omidi, Phage antibody display libraries: a powerful antibody discovery platform for immunotherapy. Crit Rev Biotechnol 2016, 36, 276.
| Phage antibody display libraries: a powerful antibody discovery platform for immunotherapy.Crossref | GoogleScholarGoogle Scholar |
[18] K Omidfar, M Daneshpour, Advances in phage display technology for drug discovery. Expert Opin Drug Discov 2015, 10, 651.
| Advances in phage display technology for drug discovery.Crossref | GoogleScholarGoogle Scholar |
[19] XD Kong, J Moriya, V Carle, F Pojer, LA Abriata, K Deyle, C Heinis, De novo development of proteolytically resistant therapeutic peptides for oral administration. Nat Biomed Eng 2020, 4, 560.
| De novo development of proteolytically resistant therapeutic peptides for oral administration.Crossref | GoogleScholarGoogle Scholar |
[20] C Heinis, T Rutherford, S Freund, G Winter, Phage-encoded combinatorial chemical libraries based on bicyclic peptides. Nat Chem Biol 2009, 5, 502.
| Phage-encoded combinatorial chemical libraries based on bicyclic peptides.Crossref | GoogleScholarGoogle Scholar |
[21] K Fosgerau, T Hoffmann, Peptide therapeutics: current status and future directions. Drug Discov Today 2015, 20, 122.
| Peptide therapeutics: current status and future directions.Crossref | GoogleScholarGoogle Scholar |
[22] JL Lau, MK Dunn, Therapeutic peptides: historical perspectives, current development trends, and future directions. Bioorg Med Chem 2018, 26, 2700.
| Therapeutic peptides: historical perspectives, current development trends, and future directions.Crossref | GoogleScholarGoogle Scholar |
[23] L Fourriere, AJ Jimenez, F Perez, G Boncompain, The role of microtubules in secretory protein transport. J Cell Sci 2020, 133, jcs237016.
| The role of microtubules in secretory protein transport.Crossref | GoogleScholarGoogle Scholar |
[24] M Matis, The mechanical role of microtubules in tissue remodeling. Bioessays 2020, 42, e1900244.
| The mechanical role of microtubules in tissue remodeling.Crossref | GoogleScholarGoogle Scholar |
[25] C Janke, MM Magiera, The tubulin code and its role in controlling microtubule properties and functions. Nat Rev Mol Cell Biol 2020, 21, 307.
| The tubulin code and its role in controlling microtubule properties and functions.Crossref | GoogleScholarGoogle Scholar |
[26] MA Jordan, L Wilson, Microtubules and actin filaments: dynamic targets for cancer chemotherapy. Curr Opin Cell Biol 1998, 10, 123.
| Microtubules and actin filaments: dynamic targets for cancer chemotherapy.Crossref | GoogleScholarGoogle Scholar |
[27] L Wilson, D Panda, MA Jordan, Modulation of microtubule dynamics by drugs: a paradigm for the actions of cellular regulators. Cell Struct Funct 1999, 24, 329.
| Modulation of microtubule dynamics by drugs: a paradigm for the actions of cellular regulators.Crossref | GoogleScholarGoogle Scholar |
[28] AM Sofias, M Dunne, G Storm, C Allen, The battle of “nano” paclitaxel. Adv Drug Deliv Rev 2017, 122, 20.
| The battle of “nano” paclitaxel.Crossref | GoogleScholarGoogle Scholar |
[29] NI Marupudi, JE Han, KW Li, VM Renard, BM Tyler, H Brem, Paclitaxel: a review of adverse toxicities and novel delivery strategies. Expert Opin Drug Saf 2007, 6, 609.
| Paclitaxel: a review of adverse toxicities and novel delivery strategies.Crossref | GoogleScholarGoogle Scholar |
[30] P Ma, RJ Mumper, Paclitaxel nano-delivery systems: a comprehensive review. J Nanomed Nanotechnol 2013, 4, 1000164.
| Paclitaxel nano-delivery systems: a comprehensive review.Crossref | GoogleScholarGoogle Scholar |
[31] H Chen, Z Lin, KE Arnst, DD Miller, W Li, Tubulin inhibitor-based antibody-drug conjugates for cancer therapy. Molecules 2017, 22, 1281.
| Tubulin inhibitor-based antibody-drug conjugates for cancer therapy.Crossref | GoogleScholarGoogle Scholar |
[32] SM Kupchan, AT Sneden, AR Branfman, GA Howie, LI Rebhun, WE Mcivor, RW Wang, TC Schnaitman, Tumor inhibitors. 124. Structural requirements for antileukemic activity among the naturally occurring and semisynthetic maytansinoids. J Med Chem 1978, 21, 31.
| Tumor inhibitors. 124. Structural requirements for antileukemic activity among the naturally occurring and semisynthetic maytansinoids.Crossref | GoogleScholarGoogle Scholar |
[33] JM Lambert, RVJ Chari, Ado-trastuzumab emtansine (T-DM1): an antibody–drug conjugate (ADC) for HER2-positive breast cancer. J Med Chem 2014, 57, 6949.
| Ado-trastuzumab emtansine (T-DM1): an antibody–drug conjugate (ADC) for HER2-positive breast cancer.Crossref | GoogleScholarGoogle Scholar |
[34] WC Widdison, SD Wilhelm, EE Cavanagh, KR Whiteman, BA Leece, Y Kovtun, VS Goldmacher, H Xie, RM Steeves, RJ Lutz, R Zhao, L Wang, WA Blättler, RVJ Chari, Semisynthetic maytansine analogues for the targeted treatment of cancer. J Med Chem 2006, 49, 4392.
| Semisynthetic maytansine analogues for the targeted treatment of cancer.Crossref | GoogleScholarGoogle Scholar |
[35] A Beck, L Goetsch, C Dumontet, N Corvaïa, Strategies and challenges for the next generation of antibody–drug conjugates. Nat Rev Drug Discov 2017, 16, 315.
| Strategies and challenges for the next generation of antibody–drug conjugates.Crossref | GoogleScholarGoogle Scholar |
[36] G Gao, Y Wang, H Hua, D Li, C Tang, Marine antitumor peptide dolastatin 10: biological activity, structural modification and synthetic chemistry. Mar Drugs 2021, 19, 363.
| Marine antitumor peptide dolastatin 10: biological activity, structural modification and synthetic chemistry.Crossref | GoogleScholarGoogle Scholar |
[37] R Bai, GR Petit, E Hamel, Dolastatin 10, a powerful cytostatic peptide derived from a marine animal: Inhibition of tubulin polymerization mediated through the vinca alkaloid binding domain. Biochem Pharmacol 1990, 39, 1941.
| Dolastatin 10, a powerful cytostatic peptide derived from a marine animal: Inhibition of tubulin polymerization mediated through the vinca alkaloid binding domain.Crossref | GoogleScholarGoogle Scholar |
[38] HC Pitot, EA Mcelroy Jr, JM Reid, AJ Windebank, JA Sloan, C Erlichman, PG Bagniewski, DL Walker, J Rubin, RM Goldberg, AA Adjei, MM Ames, Phase I trial of dolastatin-10 (NSC 376128) in patients with advanced solid tumors. Clin Cancer Res 1999, 5, 525.Available at https://www.ncbi.nlm.nih.gov/pubmed/10100703
[39] DA Garteiz, T Madden, DE Beck, WR Huie, KT Mcmanus, JL Abbruzzese, W Chen, RA Newman, Quantitation of dolastatin-10 using HPLC/electrospray ionization mass spectrometry: application in a phase I clinical trial. Cancer Chemother Pharmacol 1998, 41, 299.
| Quantitation of dolastatin-10 using HPLC/electrospray ionization mass spectrometry: application in a phase I clinical trial.Crossref | GoogleScholarGoogle Scholar |
[40] A Maderna, CA Leverett, Recent advances in the development of new auristatins: structural modifications and application in antibody drug conjugates. Mol Pharm 2015, 12, 1798.
| Recent advances in the development of new auristatins: structural modifications and application in antibody drug conjugates.Crossref | GoogleScholarGoogle Scholar |
[41] P Botella, E Rivero-Buceta, Safe approaches for camptothecin delivery: Structural analogues and nanomedicines. J Control Release 2017, 247, 28.
| Safe approaches for camptothecin delivery: Structural analogues and nanomedicines.Crossref | GoogleScholarGoogle Scholar |
[42] S Basili, S Moro, Novel camptothecin derivatives as topoisomerase I inhibitors. Expert Opin Ther Pat 2009, 19, 555.
| Novel camptothecin derivatives as topoisomerase I inhibitors.Crossref | GoogleScholarGoogle Scholar |
[43] A Hatefi, B Amsden, Camptothecin delivery methods. Pharm Res 2002, 19, 1389.
| Camptothecin delivery methods.Crossref | GoogleScholarGoogle Scholar |
[44] J Mantaj, PJM Jackson, KM Rahman, DE Thurston, From anthramycin to pyrrolobenzodiazepine (PBD)-containing antibody–drug conjugates (ADCs). Angew Chem Int Ed Engl 2017, 56, 462.
| From anthramycin to pyrrolobenzodiazepine (PBD)-containing antibody–drug conjugates (ADCs).Crossref | GoogleScholarGoogle Scholar |
[45] D Antonow, DE Thurston, Synthesis of DNA-interactive pyrrolo[2,1-c][1,4]benzodiazepines (PBDs). Chem Rev 2011, 111, 2815.
| Synthesis of DNA-interactive pyrrolo[2,1-c][1,4]benzodiazepines (PBDs).Crossref | GoogleScholarGoogle Scholar |
[46] AQ Dean, S Luo, JD Twomey, B Zhang, Targeting cancer with antibody-drug conjugates: promises and challenges. MAbs 2021, 13, 1951427.
| Targeting cancer with antibody-drug conjugates: promises and challenges.Crossref | GoogleScholarGoogle Scholar |
[47] A Mills, F Gago, Structural and mechanistic insight into DNA bending by antitumour calicheamicins. Org Biomol Chem 2021, 19, 6707.
| Structural and mechanistic insight into DNA bending by antitumour calicheamicins.Crossref | GoogleScholarGoogle Scholar |
[48] NK Damle, Tumour-targeted chemotherapy with immunoconjugates of calicheamicin. Expert Opin Biol Ther 2004, 4, 1445.
| Tumour-targeted chemotherapy with immunoconjugates of calicheamicin.Crossref | GoogleScholarGoogle Scholar |
[49] ER Boghaert, K Khandke, L Sridharan, D Armellino, M Dougher, JF Dijoseph, A Kunz, PR Hamann, A Sridharan, S Jones, C Discafani, NK Damle, Tumoricidal effect of calicheamicin immuno-conjugates using a passive targeting strategy. Int J Oncol 2006, 28, 675.Available at https://www.ncbi.nlm.nih.gov/pubmed/16465373
[50] VGS Box, The intercalation of DNA double helices with doxorubicin and nagalomycin. J Mol Graph Model 2007, 26, 14.
| The intercalation of DNA double helices with doxorubicin and nagalomycin.Crossref | GoogleScholarGoogle Scholar |
[51] C Carvalho, RX Santos, S Cardoso, S Correia, PJ Oliveira, MS Santos, PI Moreira, Doxorubicin: the good, the bad and the ugly effect. Curr Med Chem 2009, 16, 3267.
| Doxorubicin: the good, the bad and the ugly effect.Crossref | GoogleScholarGoogle Scholar |
[52] G Minotti, P Menna, E Salvatorelli, G Cairo, L Gianni, Anthracyclines: molecular advances and pharmacologic developments in antitumor activity and cardiotoxicity. Pharmacol Rev 2004, 56, 185.
| Anthracyclines: molecular advances and pharmacologic developments in antitumor activity and cardiotoxicity.Crossref | GoogleScholarGoogle Scholar |
[53] SV Liu, DD Tsao-Wei, S Xiong, S Groshen, TB Dorff, DI Quinn, YC Tai, J Engel, D Hawes, AV Schally, JK Pinski, Phase I, dose-escalation study of the targeted cytotoxic LHRH analog AEZS-108 in patients with castration- and taxane-resistant prostate cancer. Clin Cancer Res 2014, 20, 6277.
| Phase I, dose-escalation study of the targeted cytotoxic LHRH analog AEZS-108 in patients with castration- and taxane-resistant prostate cancer.Crossref | GoogleScholarGoogle Scholar |
[54] S Westphalen, G Kotulla, F Kaiser, W Krauss, G Werning, HP Elsasser, A Nagy, KD Schulz, C Grundker, AV Schally, G Emons, Receptor mediated antiproliferative effects of the cytotoxic LHRH agonist AN-152 in human ovarian and endometrial cancer cell lines. Int J Oncol 2000, 17, 1063.
| Receptor mediated antiproliferative effects of the cytotoxic LHRH agonist AN-152 in human ovarian and endometrial cancer cell lines.Crossref | GoogleScholarGoogle Scholar |
[55] P Schöffski, JP Delord, E Brain, J Robert, H Dumez, J Gasmi, A Trouet, First-in-man phase I study assessing the safety and pharmacokinetics of a 1-hour intravenous infusion of the doxorubicin prodrug DTS-201 every 3 weeks in patients with advanced or metastatic solid tumours. Eur J Cancer 2017, 86, 240.
| First-in-man phase I study assessing the safety and pharmacokinetics of a 1-hour intravenous infusion of the doxorubicin prodrug DTS-201 every 3 weeks in patients with advanced or metastatic solid tumours.Crossref | GoogleScholarGoogle Scholar |
[56] K Letschert, H Faulstich, D Keller, D Keppler, Molecular characterization and inhibition of amanitin uptake into human hepatocytes. Toxicol Sci 2006, 91, 140.
| Molecular characterization and inhibition of amanitin uptake into human hepatocytes.Crossref | GoogleScholarGoogle Scholar |
[57] A Jaeger, F Jehl, F Flesch, P Sauder, J Kopferschmitt, Kinetics of amatoxins in human poisoning: therapeutic implications. J Toxicol Clin Toxicol 1993, 31, 63.
| Kinetics of amatoxins in human poisoning: therapeutic implications.Crossref | GoogleScholarGoogle Scholar |
[58] M Muttenthaler, GF King, DJ Adams, PF Alewood, Trends in peptide drug discovery. Nat Rev Drug Discov 2021, 20, 309.
| Trends in peptide drug discovery.Crossref | GoogleScholarGoogle Scholar |
[59] D Raucher, JS Ryu, Cell-penetrating peptides: strategies for anticancer treatment. Trends Mol Med 2015, 21, 560.
| Cell-penetrating peptides: strategies for anticancer treatment.Crossref | GoogleScholarGoogle Scholar |
[60] AD Frankel, CO Pabo, Cellular uptake of the tat protein from human immunodeficiency virus. Cell 1988, 55, 1189.
| Cellular uptake of the tat protein from human immunodeficiency virus.Crossref | GoogleScholarGoogle Scholar |
[61] M Green, PM Loewenstein, Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein. Cell 1988, 55, 1179.
| Autonomous functional domains of chemically synthesized human immunodeficiency virus tat trans-activator protein.Crossref | GoogleScholarGoogle Scholar |
[62] L Zou, Q Peng, P Wang, B Zhou, Progress in research and application of HIV-1 TAT-derived cell-penetrating peptide. J Membr Biol 2017, 250, 115.
| Progress in research and application of HIV-1 TAT-derived cell-penetrating peptide.Crossref | GoogleScholarGoogle Scholar |
[63] SM Farkhani, A Valizadeh, H Karami, S Mohammadi, N Sohrabi, F Badrzadeh, Cell penetrating peptides: Efficient vectors for delivery of nanoparticles, nanocarriers, therapeutic and diagnostic molecules. Peptides 2014, 57, 78.
| Cell penetrating peptides: Efficient vectors for delivery of nanoparticles, nanocarriers, therapeutic and diagnostic molecules.Crossref | GoogleScholarGoogle Scholar |
[64] G Guidotti, L Brambilla, D Rossi, Cell-penetrating peptides: from basic research to clinics. Trends Pharmacol Sci 2017, 38, 406.
| Cell-penetrating peptides: from basic research to clinics.Crossref | GoogleScholarGoogle Scholar |
[65] K Kardani, A Milani, SH Shabani, A Bolhassani, Cell penetrating peptides: the potent multi-cargo intracellular carriers. Expert Opin Drug Deliv 2019, 16, 1227.
| Cell penetrating peptides: the potent multi-cargo intracellular carriers.Crossref | GoogleScholarGoogle Scholar |
[66] Z Su, D Xiao, F Xie, L Liu, Y Wang, S Fan, X Zhou, S Li, Antibody–drug conjugates: recent advances in linker chemistry. Acta Pharm Sin B 2021, 11, 3889.
| Antibody–drug conjugates: recent advances in linker chemistry.Crossref | GoogleScholarGoogle Scholar |
[67] Z Liu, M Xiong, J Gong, Y Zhang, N Bai, Y Luo, L Li, Y Wei, Y Liu, X Tan, R Xiang, Legumain protease-activated TAT-liposome cargo for targeting tumours and their microenvironment. Nat Commun 2014, 5, 4280.
| Legumain protease-activated TAT-liposome cargo for targeting tumours and their microenvironment.Crossref | GoogleScholarGoogle Scholar |
[68] S Majumdar, TJ Siahaan, Peptide-mediated targeted drug delivery. Med Res Rev 2012, 32, 637.
| Peptide-mediated targeted drug delivery.Crossref | GoogleScholarGoogle Scholar |
[69] GA Kuzmicheva, VA Belyavskaya, Peptide phage display in biotechnology and biomedicine. Biomed Khim 2016, 62, 481.
| Peptide phage display in biotechnology and biomedicine.Crossref | GoogleScholarGoogle Scholar |
[70] GP Smith, Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 1985, 228, 1315.
| Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface.Crossref | GoogleScholarGoogle Scholar |
[71] CH Wu, IJ Liu, RM Lu, HC Wu, Advancement and applications of peptide phage display technology in biomedical science. J Biomed Sci 2016, 23, 8.
| Advancement and applications of peptide phage display technology in biomedical science.Crossref | GoogleScholarGoogle Scholar |
[72] A Henninot, JC Collins, JM Nuss, The current state of peptide drug discovery: back to the future? J Med Chem 2018, 61, 1382.
| The current state of peptide drug discovery: back to the future?Crossref | GoogleScholarGoogle Scholar |
[73] S Katsamakas, T Chatzisideri, S Thysiadis, V Sarli, RGD-mediated delivery of small-molecule drugs. Future Med Chem 2017, 9, 579.
| RGD-mediated delivery of small-molecule drugs.Crossref | GoogleScholarGoogle Scholar |
[74] KN Sugahara, T Teesalu, PP Karmali, VR Kotamraju, L Agemy, OM Girard, D Hanahan, RF Mattrey, E Ruoslahti, Tissue-penetrating delivery of compounds and nanoparticles into tumors. Cancer Cell 2009, 16, 510.
| Tissue-penetrating delivery of compounds and nanoparticles into tumors.Crossref | GoogleScholarGoogle Scholar |
[75] KN Sugahara, T Teesalu, PP Karmali, VR Kotamraju, L Agemy, DR Greenwald, E Ruoslahti, Coadministration of a tumor-penetrating peptide enhances the efficacy of cancer drugs. Science 2010, 328, 1031.
| Coadministration of a tumor-penetrating peptide enhances the efficacy of cancer drugs.Crossref | GoogleScholarGoogle Scholar |
[76] AR Jalil, BH Hayes, JC Andrechak, Y Xia, DM Chenoweth, DE Discher, Multivalent, soluble nano-self peptides increase phagocytosis of antibody-opsonized targets while suppressing “self” signaling. ACS Nano 2020, 14, 15083.
| Multivalent, soluble nano-self peptides increase phagocytosis of antibody-opsonized targets while suppressing “self” signaling.Crossref | GoogleScholarGoogle Scholar |
[77] D Diana, C Di Salvo, V Celentano, L De Rosa, A Romanelli, R Fattorusso, LD D’Andrea, Conformational stabilization of a β-hairpin through a triazole–tryptophan interaction. Org Biomol Chem 2018, 16, 787.
| Conformational stabilization of a β-hairpin through a triazole–tryptophan interaction.Crossref | GoogleScholarGoogle Scholar |
[78] TA Stone, CM Deber, Therapeutic design of peptide modulators of protein-protein interactions in membranes. Biochim Biophys Acta Biomembr 2017, 1859, 577.
| Therapeutic design of peptide modulators of protein-protein interactions in membranes.Crossref | GoogleScholarGoogle Scholar |
[79] GE Mudd, A Brown, L Chen, K Van Rietschoten, S Watcham, DP Teufel, S Pavan, R Lani, P Huxley, GS Bennett, Identification and optimization of EphA2-selective bicycles for the delivery of cytotoxic payloads. J Med Chem 2020, 63, 4107.
| Identification and optimization of EphA2-selective bicycles for the delivery of cytotoxic payloads.Crossref | GoogleScholarGoogle Scholar |
[80] C Zhan, L Zhao, X Wei, X Wu, X Chen, W Yuan, WY Lu, M Pazgier, W Lu, An ultrahigh affinity d-peptide antagonist of MDM2. J Med Chem 2012, 55, 6237.
| An ultrahigh affinity d-peptide antagonist of MDM2.Crossref | GoogleScholarGoogle Scholar |
[81] C Li, M Pazgier, C Li, W Yuan, M Liu, G Wei, WY Lu, W Lu, Systematic mutational analysis of peptide inhibition of the p53–MDM2/MDMX interactions. J Mol Biol 2010, 398, 200.
| Systematic mutational analysis of peptide inhibition of the p53–MDM2/MDMX interactions.Crossref | GoogleScholarGoogle Scholar |
[82] X Li, N Gohain, S Chen, Y Li, X Zhao, B Li, WD Tolbert, W He, M Pazgier, H Hu, W Lu, Design of ultrahigh-affinity and dual-specificity peptide antagonists of MDM2 and MDMX for P53 activation and tumor suppression. Acta Pharm Sin B 2021, 11, 2655.
| Design of ultrahigh-affinity and dual-specificity peptide antagonists of MDM2 and MDMX for P53 activation and tumor suppression.Crossref | GoogleScholarGoogle Scholar |
[83] DJ Drucker, Advances in oral peptide therapeutics. Nat Rev Drug Discov 2020, 19, 277.
| Advances in oral peptide therapeutics.Crossref | GoogleScholarGoogle Scholar |
[84] J Hadar, S Skidmore, J Garner, H Park, K Park, Y Wang, B Qin, X Jiang, Characterization of branched poly(lactide-co-glycolide) polymers used in injectable, long-acting formulations. J Control Release 2019, 304, 75.
| Characterization of branched poly(lactide-co-glycolide) polymers used in injectable, long-acting formulations.Crossref | GoogleScholarGoogle Scholar |
[85] HN Chang, BY Liu, YK Qi, Y Zhou, YP Chen, KM Pan, WW Li, XM Zhou, WW Ma, CY Fu, YM Qi, L Liu, YF Gao, Angew Chem Int Ed Engl 2015, 54, 11760.
| Crossref | GoogleScholarGoogle Scholar |
[86] M Werle, A Bernkop-Schnürch, Strategies to improve plasma half life time of peptide and protein drugs. Amino Acids 2006, 30, 351.
| Strategies to improve plasma half life time of peptide and protein drugs.Crossref | GoogleScholarGoogle Scholar |
[87] X Zhou, C Zuo, W Li, W Shi, X Zhou, H Wang, S Chen, J Du, G Chen, W Zhai, W Zhao, Y Wu, Y Qi, L Liu, Y Gao, A novel d-peptide identified by mirror-image phage display blocks TIGIT/PVR for cancer immunotherapy. Angew Chem Int Ed Engl 2020, 59, 15114.
| A novel d-peptide identified by mirror-image phage display blocks TIGIT/PVR for cancer immunotherapy.Crossref | GoogleScholarGoogle Scholar |
[88] Y Nishimura, JN Francis, OK Donau, E Jesteadt, R Sadjadpour, AR Smith, MS Seaman, BD Welch, MA Martin, MS Kay, Prevention and treatment of SHIVAD8 infection in rhesus macaques by a potent d-peptide HIV entry inhibitor. Proc Natl Acad Sci U S A 2020, 117, 22436.
| Prevention and treatment of SHIVAD8 infection in rhesus macaques by a potent d-peptide HIV entry inhibitor.Crossref | GoogleScholarGoogle Scholar |
[89] Y Zhang, M Ouyang, H Wang, B Zhang, W Guang, R Liu, X Li, TC Shih, Z Li, J Cao, Q Meng, Z Su, J Ye, F Liu, A Hong, X Chen, A cyclic peptide retards the proliferation of DU145 prostate cancer cells in vitro and in vivo through inhibition of FGFR2. MedComm 2020, 1, 362.
| A cyclic peptide retards the proliferation of DU145 prostate cancer cells in vitro and in vivo through inhibition of FGFR2.Crossref | GoogleScholarGoogle Scholar |
[90] Naloxegol (Movantik) for opioid-induced constipation. JAMA 2016, 315, 194.
| Naloxegol (Movantik) for opioid-induced constipation.Crossref | GoogleScholarGoogle Scholar |
[91] I Bjørnsdottir, B Støvring, T Søeborg, H Jacobsen, O Sternebring, Plasma polyethylene glycol (PEG) levels reach steady state following repeated treatment with N8-GP (Turoctocog Alfa Pegol; Esperoct®). Drugs R D 2020, 20, 75.
| Plasma polyethylene glycol (PEG) levels reach steady state following repeated treatment with N8-GP (Turoctocog Alfa Pegol; Esperoct®).Crossref | GoogleScholarGoogle Scholar |
[92] LB Knudsen, J Lau, The discovery and development of liraglutide and semaglutide. Front Endocrinol (Lausanne) 2019, 10, 155.
| The discovery and development of liraglutide and semaglutide.Crossref | GoogleScholarGoogle Scholar |
[93] BM Cooper, J Iegre, DH O’Donovan, M Ölwegård Halvarsson, DR Spring, Peptides as a platform for targeted therapeutics for cancer: peptide–drug conjugates (PDCs). Chem Soc Rev 2021, 50, 1480.
| Peptides as a platform for targeted therapeutics for cancer: peptide–drug conjugates (PDCs).Crossref | GoogleScholarGoogle Scholar |
[94] I Vhora, S Patil, P Bhatt, A Misra, Chapter one - protein– and peptide–drug conjugates: an emerging drug delivery technology. Adv Protein Chem Struct Biol 2015, 98, 1.
| Chapter one - protein– and peptide–drug conjugates: an emerging drug delivery technology.Crossref | GoogleScholarGoogle Scholar |
[95] V Chudasama, A Maruani, S Caddick, Recent advances in the construction of antibody–drug conjugates. Nat Chem 2016, 8, 114.
| Recent advances in the construction of antibody–drug conjugates.Crossref | GoogleScholarGoogle Scholar |
[96] Y Chu, X Zhou, X Wang, Antibody-drug conjugates for the treatment of lymphoma: clinical advances and latest progress. J Hematol Oncol 2021, 14, 88.
| Antibody-drug conjugates for the treatment of lymphoma: clinical advances and latest progress.Crossref | GoogleScholarGoogle Scholar |
[97] V Kostova, P Désos, JB Starck, A Kotschy, The chemistry behind ADCs. Pharmaceuticals (Basel) 2021, 14, 442.
| The chemistry behind ADCs.Crossref | GoogleScholarGoogle Scholar |
[98] VHJ van der Velden, JG Te Marvelde, PG Hoogeveen, ID Bernstein, AB Houtsmuller, MS Berger, JJM van Dongen, Targeting of the CD33-calicheamicin immunoconjugate Mylotarg (CMA-676) in acute myeloid leukemia: in vivo and in vitro saturation and internalization by leukemic and normal myeloid cells. Blood 2001, 97, 3197.
| Targeting of the CD33-calicheamicin immunoconjugate Mylotarg (CMA-676) in acute myeloid leukemia: in vivo and in vitro saturation and internalization by leukemic and normal myeloid cells.Crossref | GoogleScholarGoogle Scholar |
[99] HK Erickson, PU Park, WC Widdison, YV Kovtun, LM Garrett, K Hoffman, RJ Lutz, VS Goldmacher, WA Blättler, Antibody–maytansinoid conjugates are activated in targeted cancer cells by lysosomal degradation and linker-dependent intracellular processing. Cancer Res 2006, 66, 4426.
| Antibody–maytansinoid conjugates are activated in targeted cancer cells by lysosomal degradation and linker-dependent intracellular processing.Crossref | GoogleScholarGoogle Scholar |
[100] F Li, J Lu, J Liu, C Liang, M Wang, L Wang, D Li, H Yao, Q Zhang, J Wen, ZK Zhang, J Li, Q Lv, X He, B Guo, D Guan, Y Yu, L Dang, X Wu, Y Li, G Chen, F Jiang, S Sun, BT Zhang, A Lu, G Zhang, A water-soluble nucleolin aptamer–paclitaxel conjugate for tumor-specific targeting in ovarian cancer. Nat Commun 2017, 8, 1390.
| A water-soluble nucleolin aptamer–paclitaxel conjugate for tumor-specific targeting in ovarian cancer.Crossref | GoogleScholarGoogle Scholar |
[101] SH Kim, JA Kaplan, Y Sun, A Shieh, HL Sun, CM Croce, MW Grinstaff, JR Parquette, The self-assembly of anticancer camptothecin–dipeptide nanotubes: a minimalistic and high drug loading approach to increased efficacy. Chem Eur J 2015, 21, 101.
| The self-assembly of anticancer camptothecin–dipeptide nanotubes: a minimalistic and high drug loading approach to increased efficacy.Crossref | GoogleScholarGoogle Scholar |
[102] M Jamous, U Haberkorn, W Mier, Synthesis of peptide radiopharmaceuticals for the therapy and diagnosis of tumor diseases. Molecules 2013, 18, 3379.
| Synthesis of peptide radiopharmaceuticals for the therapy and diagnosis of tumor diseases.Crossref | GoogleScholarGoogle Scholar |
[103] M Poreba, Recent advances in the development of legumain-selective chemical probes and peptide prodrugs. Biol Chem 2019, 400, 1529.
| Recent advances in the development of legumain-selective chemical probes and peptide prodrugs.Crossref | GoogleScholarGoogle Scholar |
[104] S Majumdar, N Kobayashi, JP Krise, TJ Siahaan, Mechanism of internalization of an ICAM-1-derived peptide by human leukemic cell line HL-60: influence of physicochemical properties on targeted drug delivery. Mol Pharm 2007, 4, 749.
| Mechanism of internalization of an ICAM-1-derived peptide by human leukemic cell line HL-60: influence of physicochemical properties on targeted drug delivery.Crossref | GoogleScholarGoogle Scholar |
[105] C-S Jiang, WEG Müller, HC Schröder, Y-W Guo, Disulfide- and multisulfide-containing metabolites from marine organisms. Chem Rev 2012, 112, 2179.
| Disulfide- and multisulfide-containing metabolites from marine organisms.Crossref | GoogleScholarGoogle Scholar |
[106] I Ojima, Guided molecular missiles for tumor-targeting chemotherapy – case studies using the second-generation taxoids as warheads. Acc Chem Res 2008, 41, 108.
| Guided molecular missiles for tumor-targeting chemotherapy – case studies using the second-generation taxoids as warheads.Crossref | GoogleScholarGoogle Scholar |
[107] MH Lee, Z Yang, CW Lim, YH Lee, S Dongbang, C Kang, JS Kim, Disulfide-cleavage-triggered chemosensors and their biological applications. Chem Rev 2013, 113, 5071.
| Disulfide-cleavage-triggered chemosensors and their biological applications.Crossref | GoogleScholarGoogle Scholar |
[108] P Zhang, J Wu, F Xiao, D Zhao, Y Luan, Disulfide bond based polymeric drug carriers for cancer chemotherapy and relevant redox environments in mammals. Med Res Rev 2018, 38, 1485.
| Disulfide bond based polymeric drug carriers for cancer chemotherapy and relevant redox environments in mammals.Crossref | GoogleScholarGoogle Scholar |
[109] RVJ Chari, ML Miller, WC Widdison, Antibody–drug conjugates: an emerging concept in cancer therapy. Angew Chem Int Ed Engl 2014, 53, 3796.
| Antibody–drug conjugates: an emerging concept in cancer therapy.Crossref | GoogleScholarGoogle Scholar |
[110] D Zhang, GB Qi, YX Zhao, SL Qiao, C Yang, H Wang, In situ formation of nanofibers from purpurin18–peptide conjugates and the assembly induced retention effect in tumor sites. Adv Mater 2015, 27, 6125.
| In situ formation of nanofibers from purpurin18–peptide conjugates and the assembly induced retention effect in tumor sites.Crossref | GoogleScholarGoogle Scholar |
[111] DB Cheng, D Wang, YJ Gao, L Wang, ZY Qiao, H Wang, Autocatalytic morphology transformation platform for targeted drug accumulation. J Am Chem Soc 2019, 141, 4406.
| Autocatalytic morphology transformation platform for targeted drug accumulation.Crossref | GoogleScholarGoogle Scholar |
[112] D Dornan, F Bennett, Y Chen, M Dennis, D Eaton, K Elkins, D French, MAT Go, A Jack, JR Junutula, H Koeppen, J Lau, J Mcbride, A Rawstron, X Shi, N Yu, SF Yu, P Yue, B Zheng, A Ebens, AG Polson, Therapeutic potential of an anti-CD79b antibody–drug conjugate, anti–CD79b-vc-MMAE, for the treatment of non-Hodgkin lymphoma. Blood 2009, 114, 2721.
| Therapeutic potential of an anti-CD79b antibody–drug conjugate, anti–CD79b-vc-MMAE, for the treatment of non-Hodgkin lymphoma.Crossref | GoogleScholarGoogle Scholar |
[113] B Nolting, Linker technologies for antibody–drug conjugates. Methods Mol Biol 2013, 1045, 71.
| Linker technologies for antibody–drug conjugates.Crossref | GoogleScholarGoogle Scholar |
[114] HM Kantarjian, DJ Deangelo, M Stelljes, G Martinelli, M Liedtke, W Stock, N Gökbuget, S O’Brien, K Wang, T Wang, ML Paccagnella, B Sleight, E Vandendries, AS Advani, Inotuzumab ozogamicin versus standard therapy for acute lymphoblastic leukemia. N Engl J Med 2016, 375, 740.
| Inotuzumab ozogamicin versus standard therapy for acute lymphoblastic leukemia.Crossref | GoogleScholarGoogle Scholar |
[115] A Nagy, AV Schally, P Armatis, K Szepeshazi, G Halmos, M Kovacs, M Zarandi, K Groot, M Miyazaki, A Jungwirth, J Horvath, Cytotoxic analogs of luteinizing hormone-releasing hormone containing doxorubicin or 2-pyrrolinodoxorubicin, a derivative 500-1000 times more potent. Proc Natl Acad Sci U S A 1996, 93, 7269.
| Cytotoxic analogs of luteinizing hormone-releasing hormone containing doxorubicin or 2-pyrrolinodoxorubicin, a derivative 500-1000 times more potent.Crossref | GoogleScholarGoogle Scholar |
[116] H Zhang, K Wang, K Na, D Li, Z Li, D Zhao, L Zhong, M Wang, L Kou, C Luo, H Zhang, Q Kan, H Ding, Z He, J Sun, Striking a balance between carbonate/carbamate linkage bond- and reduction-sensitive disulfide bond-bearing linker for tailored controlled release: in situ covalent-albumin-binding gemcitabine prodrugs promote bioavailability and tumor accumulation. J Med Chem 2018, 61, 4904.
| Striking a balance between carbonate/carbamate linkage bond- and reduction-sensitive disulfide bond-bearing linker for tailored controlled release: in situ covalent-albumin-binding gemcitabine prodrugs promote bioavailability and tumor accumulation.Crossref | GoogleScholarGoogle Scholar |
[117] E Ziaei, A Saghaeidehkordi, C Dill, I Maslennikov, S Chen, K Kaur, Targeting triple negative breast cancer cells with novel cytotoxic peptide–doxorubicin conjugates. Bioconjug Chem 2019, 30, 3098.
| Targeting triple negative breast cancer cells with novel cytotoxic peptide–doxorubicin conjugates.Crossref | GoogleScholarGoogle Scholar |
[118] N Jain, SW Smith, S Ghone, B Tomczuk, Current ADC linker chemistry. Pharm Res 2015, 32, 3526.
| Current ADC linker chemistry.Crossref | GoogleScholarGoogle Scholar |
[119] R Voelker, First radioactive drug for adults with rare cancer. JAMA 2018, 319, 857.
| First radioactive drug for adults with rare cancer.Crossref | GoogleScholarGoogle Scholar |
[120] E Murphy, EE Prommer, M Mihalyo, A Wilcock, Octreotide. J Pain Symptom Manage 2010, 40, 142.
| Octreotide.Crossref | GoogleScholarGoogle Scholar |
[121] P Musto, F D’Auria, Melphalan: old and new uses of a still master drug for multiple myeloma. Expert Opin Investig Drugs 2007, 16, 1467.
| Melphalan: old and new uses of a still master drug for multiple myeloma.Crossref | GoogleScholarGoogle Scholar |
[122] G Sarosy, B Leyland-Jones, P Soochan, BD Cheson, The systemic administration of intravenous melphalan. J Clin Oncol 1988, 6, 1768.
| The systemic administration of intravenous melphalan.Crossref | GoogleScholarGoogle Scholar |
[123] MV Mateos, MA Dimopoulos, M Cavo, K Suzuki, A Jakubowiak, S Knop, C Doyen, P Lucio, Z Nagy, P Kaplan, L Pour, M Cook, S Grosicki, A Crepaldi, AM Liberati, P Campbell, T Shelekhova, SS Yoon, G Iosava, T Fujisaki, M Garg, C Chiu, J Wang, R Carson, W Crist, W Deraedt, H Nguyen, M Qi, J San-Miguel, Daratumumab plus bortezomib, melphalan, and prednisone for untreated myeloma. N Engl J Med 2018, 378, 518.
| Daratumumab plus bortezomib, melphalan, and prednisone for untreated myeloma.Crossref | GoogleScholarGoogle Scholar |
[124] M Wickström, C Haglund, H Lindman, P Nygren, R Larsson, J Gullbo, The novel alkylating prodrug J1: diagnosis directed activity profile ex vivo and combination analyses in vitro. Invest New Drugs 2008, 26, 195.
| The novel alkylating prodrug J1: diagnosis directed activity profile ex vivo and combination analyses in vitro.Crossref | GoogleScholarGoogle Scholar |
[125] MV Mateos, J Bladé, S Bringhen, EM Ocio, Y Efebera, L Pour, F Gay, P Sonneveld, J Gullbo, PG Richardson, Melflufen: a peptide–drug conjugate for the treatment of multiple myeloma. J Clin Med 2020, 9, 3120.
| Melflufen: a peptide–drug conjugate for the treatment of multiple myeloma.Crossref | GoogleScholarGoogle Scholar |
[126] M Delforoush, S Strese, M Wickström, R Larsson, G Enblad, J Gullbo, In vitro and in vivo activity of melflufen (J1) in lymphoma. BMC Cancer 2016, 16, 263.
| In vitro and in vivo activity of melflufen (J1) in lymphoma.Crossref | GoogleScholarGoogle Scholar |
[127] PG Richardson, A Oriol, A Larocca, J Bladé, M Cavo, P Rodriguez-Otero, X Leleu, O Nadeem, JW Hiemenz, H Hassoun, C Touzeau, A Alegre, A Paner, C Maisel, A Mazumder, A Raptis, JS Moreb, KC Anderson, JP Laubach, S Thuresson, M Thuresson, C Byrne, J Harmenberg, NA Bakker, MV Mateos, Melflufen and dexamethasone in heavily pretreated relapsed and refractory multiple myeloma. J Clin Oncol 2021, 39, 757.
| Melflufen and dexamethasone in heavily pretreated relapsed and refractory multiple myeloma.Crossref | GoogleScholarGoogle Scholar |
[128] AV Schally, NL Block, FG Rick, Discovery of LHRH and development of LHRH analogs for prostate cancer treatment. Prostate 2017, 77, 1036.
| Discovery of LHRH and development of LHRH analogs for prostate cancer treatment.Crossref | GoogleScholarGoogle Scholar |
[129] V Maclachlan, M Besanko, F O’Shea, H Wade, C Wood, A Trounson, DL Healy, A controlled study of luteinizing hormone–releasing hormone agonist (Buserelin) for the induction of folliculogenesis before in vitro fertilization. N Engl J Med 1989, 320, 1233.
| A controlled study of luteinizing hormone–releasing hormone agonist (Buserelin) for the induction of folliculogenesis before in vitro fertilization.Crossref | GoogleScholarGoogle Scholar |
[130] RM Kelly, SL Highfill, A Panoskaltsis-Mortari, PA Taylor, RL Boyd, GA Holländer, BR Blazar, Keratinocyte growth factor and androgen blockade work in concert to protect against conditioning regimen-induced thymic epithelial damage and enhance T-cell reconstitution after murine bone marrow transplantation. Blood 2008, 111, 5734.
| Keratinocyte growth factor and androgen blockade work in concert to protect against conditioning regimen-induced thymic epithelial damage and enhance T-cell reconstitution after murine bone marrow transplantation.Crossref | GoogleScholarGoogle Scholar |
[131] G Oláh, N Dobos, G Vámosi, Z Szabó, É Sipos, K Fodor, K Harda, AV Schally, G Halmos, Experimental therapy of doxorubicin resistant human uveal melanoma with targeted cytotoxic luteinizing hormone-releasing hormone analog (AN-152). Eur J Pharm Sci 2018, 123, 371.
| Experimental therapy of doxorubicin resistant human uveal melanoma with targeted cytotoxic luteinizing hormone-releasing hormone analog (AN-152).Crossref | GoogleScholarGoogle Scholar |
[132] X Wang, LJ Krebs, M Al-Nuri, HE Pudavar, S Ghosal, C Liebow, AA Nagy, AV Schally, PN Prasad, A chemically labeled cytotoxic agent: Two-photon fluorophore for optical tracking of cellular pathway in chemotherapy. Proc Natl Acad Sci U S A 1999, 96, 11081.
| A chemically labeled cytotoxic agent: Two-photon fluorophore for optical tracking of cellular pathway in chemotherapy.Crossref | GoogleScholarGoogle Scholar |
[133] G Emons, G Gorchev, J Sehouli, P Wimberger, A Stähle, L Hanker, F Hilpert, H Sindermann, C Gründker, P Harter, Efficacy and safety of AEZS-108 (INN: Zoptarelin Doxorubicin acetate) an LHRH agonist linked to doxorubicin in women with platinum refractory or resistant ovarian cancer expressing LHRH receptors: a multicenter Phase II trial of the ago-study group (AGO GYN 5). Gynecol Oncol 2014, 133, 427.
| Efficacy and safety of AEZS-108 (INN: Zoptarelin Doxorubicin acetate) an LHRH agonist linked to doxorubicin in women with platinum refractory or resistant ovarian cancer expressing LHRH receptors: a multicenter Phase II trial of the ago-study group (AGO GYN 5).Crossref | GoogleScholarGoogle Scholar |
[134] G Emons, G Gorchev, P Harter, P Wimberger, A Stähle, L Hanker, F Hilpert, MW Beckmann, P Dall, C Gründker, H Sindermann, J Sehouli, Efficacy and safety of AEZS-108 (LHRH agonist linked to Doxorubicin) in women with advanced or recurrent endometrial cancer expressing LHRH receptors: a multicenter phase 2 trial (AGO-GYN5). Int J Gynecol Cancer 2014, 24, 260.
| Efficacy and safety of AEZS-108 (LHRH agonist linked to Doxorubicin) in women with advanced or recurrent endometrial cancer expressing LHRH receptors: a multicenter phase 2 trial (AGO-GYN5).Crossref | GoogleScholarGoogle Scholar |
[135] FC Thomas, K Taskar, V Rudraraju, S Goda, HR Thorsheim, JA Gaasch, RK Mittapalli, D Palmieri, PS Steeg, PR Lockman, QR Smith, Uptake of ANG1005, a novel paclitaxel derivative, through the blood-brain barrier into brain and experimental brain metastases of breast cancer. Pharm Res 2009, 26, 2486.
| Uptake of ANG1005, a novel paclitaxel derivative, through the blood-brain barrier into brain and experimental brain metastases of breast cancer.Crossref | GoogleScholarGoogle Scholar |
[136] P Kumthekar, SC Tang, AJ Brenner, S Kesari, DE Piccioni, C Anders, J Carrillo, P Chalasani, P Kabos, S Puhalla, K Tkaczuk, AA Garcia, MS Ahluwalia, JS Wefel, N Lakhani, N Ibrahim, Clin Cancer Res 2020, 26, 2789.
| Crossref | GoogleScholarGoogle Scholar |
[137] A Régina, M Demeule, C Ché, I Lavallée, J Poirier, R Gabathuler, R Béliveau, JP Castaigne, Antitumour activity of ANG1005, a conjugate between paclitaxel and the new brain delivery vector Angiopep-2. Br J Pharmacol 2008, 155, 185.
| Antitumour activity of ANG1005, a conjugate between paclitaxel and the new brain delivery vector Angiopep-2.Crossref | GoogleScholarGoogle Scholar |
[138] R Soffietti, M Ahluwalia, N Lin, R Rudà, Management of brain metastases according to molecular subtypes. Nat Rev Neurol 2020, 16, 557.
| Management of brain metastases according to molecular subtypes.Crossref | GoogleScholarGoogle Scholar |
[139] F Li, SC Tang, Targeting metastatic breast cancer with ANG1005, a novel peptide-paclitaxel conjugate that crosses the blood-brain-barrier (BBB). Genes Dis 2017, 4, 1.
| Targeting metastatic breast cancer with ANG1005, a novel peptide-paclitaxel conjugate that crosses the blood-brain-barrier (BBB).Crossref | GoogleScholarGoogle Scholar |
[140] T Zimmermann, P Drašar, S Rimpelová, SB Christensen, VA Khripach, M Jurášek, Large scale conversion of trilobolide into the payload of mipsagargin: 8-O-(12-aminododecanoyl)-8-O-debutanoylthapsigargin. Biomolecules 2020, 10, 1640.
| Large scale conversion of trilobolide into the payload of mipsagargin: 8-O-(12-aminododecanoyl)-8-O-debutanoylthapsigargin.Crossref | GoogleScholarGoogle Scholar |
[141] TB Andersen, CQ López, T Manczak, K Martinez, HT Simonsen, Thapsigargin – from Thapsia L. to mipsagargin. Molecules 2015, 20, 6113.
| Thapsigargin – from Thapsia L. to mipsagargin.Crossref | GoogleScholarGoogle Scholar |
[142] SR Denmeade, AM Mhaka, DM Rosen, WN Brennen, S Dalrymple, I Dach, C Olesen, B Gurel, AM Demarzo, G Wilding, MA Carducci, CA Dionne, JV Møller, P Nissen, SB Christensen, JT Isaacs, Engineering a prostate-specific membrane antigen–activated tumor endothelial cell prodrug for cancer therapy. Sci Transl Med 2012, 4, 140ra86.
| Engineering a prostate-specific membrane antigen–activated tumor endothelial cell prodrug for cancer therapy.Crossref | GoogleScholarGoogle Scholar |
[143] A Jaskulska, AE Janecka, K Gach-Janczak, Thapsigargin – from traditional medicine to anticancer drug. Int J Mol Sci 2020, 22, 4.
| Thapsigargin – from traditional medicine to anticancer drug.Crossref | GoogleScholarGoogle Scholar |
[144] AP Davenport, CCG Scully, C De Graaf, AJH Brown, JJ Maguire, Advances in therapeutic peptides targeting G protein-coupled receptors. Nat Rev Drug Discov 2020, 19, 389.
| Advances in therapeutic peptides targeting G protein-coupled receptors.Crossref | GoogleScholarGoogle Scholar |
[145] AV Schally, A Nagy, New approaches to treatment of various cancers based on cytotoxic analogs of LHRH, somatostatin and bombesin. Life Sci 2003, 72, 2305.
| New approaches to treatment of various cancers based on cytotoxic analogs of LHRH, somatostatin and bombesin.Crossref | GoogleScholarGoogle Scholar |
[146] KK Curtis, J Sarantopoulos, DW Northfelt, GJ Weiss, KM Barnhart, JK Whisnant, C Leuschner, H Alila, MJ Borad, RK Ramanathan, Novel LHRH-receptor-targeted cytolytic peptide, EP-100: first-in-human phase I study in patients with advanced LHRH-receptor-expressing solid tumors. Cancer Chemother Pharmacol 2014, 73, 931.
| Novel LHRH-receptor-targeted cytolytic peptide, EP-100: first-in-human phase I study in patients with advanced LHRH-receptor-expressing solid tumors.Crossref | GoogleScholarGoogle Scholar |
[147] C Leuschner, W Hansel, Membrane disrupting lytic peptides for cancer treatments. Curr Pharm Des 2004, 10, 2299.
| Membrane disrupting lytic peptides for cancer treatments.Crossref | GoogleScholarGoogle Scholar |
[148] SY Shin, JH Kang, SY Jang, Y Kim, KL Kim, KS Hahm, Effects of the hinge region of cecropin A(1–8)–magainin 2(1–12), a synthetic antimicrobial peptide, on liposomes, bacterial and tumor cells. Biochim Biophys Acta Biomembr 2000, 1463, 209.
| Effects of the hinge region of cecropin A(1–8)–magainin 2(1–12), a synthetic antimicrobial peptide, on liposomes, bacterial and tumor cells.Crossref | GoogleScholarGoogle Scholar |
[149] N Yang, Ø Rekdal, W Stensen, JS Svendsen, Enhanced antitumor activity and selectivity of lactoferrin-derived peptides. J Pept Res 2002, 60, 187.
| Enhanced antitumor activity and selectivity of lactoferrin-derived peptides.Crossref | GoogleScholarGoogle Scholar |
[150] MS Kim, S Ma, A Chelariu-Raicu, C Leuschner, HW Alila, S Lee, RL Coleman, AK Sood, Enhanced immunotherapy with LHRH-R targeted lytic peptide in ovarian cancer. Mol Cancer Ther 2020, 19, 2396.
| Enhanced immunotherapy with LHRH-R targeted lytic peptide in ovarian cancer.Crossref | GoogleScholarGoogle Scholar |
[151] A Chelariu-Raicu, A Nick, R Urban, M Gordinier, C Leuschner, L Bavisotto, GZD Molin, JK Whisnant, RL Coleman, A multicenter open-label randomized phase II trial of paclitaxel plus EP-100, a novel LHRH receptor-targeted, membrane-disrupting peptide, versus paclitaxel alone for refractory or recurrent ovarian cancer. Gynecol Oncol 2021, 160, 418.
| A multicenter open-label randomized phase II trial of paclitaxel plus EP-100, a novel LHRH receptor-targeted, membrane-disrupting peptide, versus paclitaxel alone for refractory or recurrent ovarian cancer.Crossref | GoogleScholarGoogle Scholar |
[152] KM Tyner, SR Schiffman, EP Giannelis, Nanobiohybrids as delivery vehicles for camptothecin. J Control Release 2004, 95, 501.
| Nanobiohybrids as delivery vehicles for camptothecin.Crossref | GoogleScholarGoogle Scholar |
[153] K Lackey, JM Besterman, W Fletcher, P Leitner, B Morton, DD Sternbach, Rigid analogs of camptothecin as DNA topoisomerase I inhibitors. J Med Chem 1995, 38, 906.
| Rigid analogs of camptothecin as DNA topoisomerase I inhibitors.Crossref | GoogleScholarGoogle Scholar |
[154] BS Lee, AK Nalla, IR Stock, TC Shear, KL Black, JS Yu, Oxidative stimuli-responsive nanoprodrug of camptothecin kills glioblastoma cells. Bioorg Med Chem Lett 2010, 20, 5262.
| Oxidative stimuli-responsive nanoprodrug of camptothecin kills glioblastoma cells.Crossref | GoogleScholarGoogle Scholar |
[155] M Martínez-Martínez, G Rodríguez-Berna, M Bermejo, I Gonzalez-Alvarez, M Gonzalez-Alvarez, V Merino, Covalently crosslinked organophosphorous derivatives-chitosan hydrogel as a drug delivery system for oral administration of camptothecin. Eur J Pharm Biopharm 2019, 136, 174.
| Covalently crosslinked organophosphorous derivatives-chitosan hydrogel as a drug delivery system for oral administration of camptothecin.Crossref | GoogleScholarGoogle Scholar |
[156] A Guiotto, M Canevari, P Orsolini, O Lavanchy, C Deuschel, N Kaneda, A Kurita, T Matsuzaki, T Yaegashi, S Sawada, FM Veronese, Efficient and chemoselective N-acylation of 10-amino-7-ethyl camptothecin with poly(ethylene glycol). Bioorg Med Chem Lett 2004, 14, 1803.
| Efficient and chemoselective N-acylation of 10-amino-7-ethyl camptothecin with poly(ethylene glycol).Crossref | GoogleScholarGoogle Scholar |
[157] CT Zi, L Yang, FQ Xu, FW Dong, RJ Ma, Y Li, J Zhou, ZT Ding, ZH Jiang, JM Hu, Synthesis and antitumor activity of biotinylated camptothecin derivatives as potent cytotoxic agents. Bioorg Med Chem Lett 2019, 29, 234.
| Synthesis and antitumor activity of biotinylated camptothecin derivatives as potent cytotoxic agents.Crossref | GoogleScholarGoogle Scholar |
[158] CJ Thomas, NJ Rahier, SM Hecht, Camptothecin: current perspectives. Bioorg Med Chem 2004, 12, 1585.
| Camptothecin: current perspectives.Crossref | GoogleScholarGoogle Scholar |
[159] F Meyer-Losic, C Nicolazzi, J Quinonero, F Ribes, M Michel, V Dubois, C De Coupade, M Boukaissi, A-S Che’ne’, I Tranchant, V Arranz, I Zoubaa, J-S Fruchart, D Ravel, J Kearsey, DTS-108, a novel peptidic prodrug of SN38: in vivo efficacy and toxicokinetic studies. Clin Cancer Res 2008, 14, 2145.
| DTS-108, a novel peptidic prodrug of SN38: in vivo efficacy and toxicokinetic studies.Crossref | GoogleScholarGoogle Scholar |
[160] R Coriat, SJ Faivre, O Mir, C Dreyer, S Ropert, M Bouattour, R Desjardins, F Goldwasser, E Raymond, Pharmacokinetics and safety of DTS-108, a human oligopeptide bound to SN-38 with an esterase-sensitive cross-linker in patients with advanced malignancies: a Phase I study. Int J Nanomedicine 2016, 11, 6207.
| Pharmacokinetics and safety of DTS-108, a human oligopeptide bound to SN-38 with an esterase-sensitive cross-linker in patients with advanced malignancies: a Phase I study.Crossref | GoogleScholarGoogle Scholar |
[161] T Suzuki, S Futaki, M Niwa, S Tanaka, K Ueda, Y Sugiura, Possible existence of common internalization mechanisms among arginine-rich peptides. J Biol Chem 2002, 277, 2437.
| Possible existence of common internalization mechanisms among arginine-rich peptides.Crossref | GoogleScholarGoogle Scholar |
[162] S Futaki, S Goto, Y Sugiura, Membrane permeability commonly shared among arginine-rich peptides. J Mol Recognit 2003, 16, 260.
| Membrane permeability commonly shared among arginine-rich peptides.Crossref | GoogleScholarGoogle Scholar |
[163] J Cornillie, A Wozniak, P Pokreisz, A Casazza, L Vreys, J Wellens, U Vanleeuw, YK Gebreyohannes, M Debiec-Rychter, R Sciot, D Hompes, P Schöffski, In vivo antitumoral efficacy of PhAc-ALGP-doxorubicin, an enzyme-activated doxorubicin prodrug, in patient-derived soft tissue sarcoma xenograft models. Mol Cancer Ther 2017, 16, 1566.
| In vivo antitumoral efficacy of PhAc-ALGP-doxorubicin, an enzyme-activated doxorubicin prodrug, in patient-derived soft tissue sarcoma xenograft models.Crossref | GoogleScholarGoogle Scholar |
[164] EM Driggers, SP Hale, J Lee, NK Terrett, The exploration of macrocycles for drug discovery — an underexploited structural class. Nat Rev Drug Discov 2008, 7, 608.
| The exploration of macrocycles for drug discovery — an underexploited structural class.Crossref | GoogleScholarGoogle Scholar |
[165] RJ Cherney, L Wang, DT Meyer, CB Xue, ZR Wasserman, KD Hardman, PK Welch, MB Covington, RA Copeland, EC Arner, WF Degrado, CP Decicco, Macrocyclic amino carboxylates as selective MMP-8 inhibitors. J Med Chem 1998, 41, 1749.
| Macrocyclic amino carboxylates as selective MMP-8 inhibitors.Crossref | GoogleScholarGoogle Scholar |
[166] MC Vos, AAM Van Der Wurff, TH Van Kuppevelt, LFAG Massuger, The role of MMP-14 in ovarian cancer: a systematic review. J Ovarian Res 2021, 14, 101.
| The role of MMP-14 in ovarian cancer: a systematic review.Crossref | GoogleScholarGoogle Scholar |
[167] G Bennett, A Brown, G Mudd, P Huxley, K Van Rietschoten, S Pavan, L Chen, S Watcham, J Lahdenranta, N Keen, MMAE delivery using the bicycle toxin conjugate BT5528. Mol Cancer Ther 2020, 19, 1385.
| MMAE delivery using the bicycle toxin conjugate BT5528.Crossref | GoogleScholarGoogle Scholar |
[168] S Roselli, J Pundavela, Y Demont, S Faulkner, S Keene, J Attia, CC Jiang, XD Zhang, MM Walker, H Hondermarck, Sortilin is associated with breast cancer aggressiveness and contributes to tumor cell adhesion and invasion. Oncotarget 2015, 6, 10473.
| Sortilin is associated with breast cancer aggressiveness and contributes to tumor cell adhesion and invasion.Crossref | GoogleScholarGoogle Scholar |
[169] M Demeule, C Charfi, J-C Currie, A Larocque, A Zgheib, S Kozelko, R Béliveau, C Marsolais, B Annabi, TH1902, a new docetaxel-peptide conjugate for the treatment of sortilin-positive triple-negative breast cancer. Cancer Sci 2021, 112, 4317.
| TH1902, a new docetaxel-peptide conjugate for the treatment of sortilin-positive triple-negative breast cancer.Crossref | GoogleScholarGoogle Scholar |
[170] J Delahousse, C Skarbek, A Paci, Prodrugs as drug delivery system in oncology. Cancer Chemother Pharmacol 2019, 84, 937.
| Prodrugs as drug delivery system in oncology.Crossref | GoogleScholarGoogle Scholar |
[171] C Do Pazo, K Nawaz, RM Webster, The oncology market for antibody–drug conjugates. Nat Rev Drug Discov 2021, 20, 583.
| The oncology market for antibody–drug conjugates.Crossref | GoogleScholarGoogle Scholar |
[172] SS Kale, C Villequey, XD Kong, A Zorzi, K Deyle, C Heinis, Cyclization of peptides with two chemical bridges affords large scaffold diversities. Nat Chem 2018, 10, 715.
| Cyclization of peptides with two chemical bridges affords large scaffold diversities.Crossref | GoogleScholarGoogle Scholar |
[173] NTQ Doan, ES Paulsen, P Sehgal, JV Møller, P Nissen, SR Denmeade, JT Isaacs, CA Dionne, SB Christensen, Targeting thapsigargin towards tumors. Steroids 2015, 97, 2.
| Targeting thapsigargin towards tumors.Crossref | GoogleScholarGoogle Scholar |
