Nuclear Magnetic Resonance Study of the Peptide FRANCESSEPAROVIC
John A. Karas A , David W. Keizer B and Marc-Antoine Sani
B C D
A Department of Pharmacology and Therapeutics, School of Biomedical Sciences, Faculty of Medicine, Dentistry and Health Sciences, The University of Melbourne, Parkville, Vic. 3010, Australia.
B Bio21 Institute, The University of Melbourne, Parkville, Vic. 3010, Australia.
C School of Chemistry, The University of Melbourne, Parkville, Vic. 3010, Australia.
D Corresponding author. Email: msani@unimelb.edu.au
Australian Journal of Chemistry 73(3) 158-163 https://doi.org/10.1071/CH19357
Submitted: 30 July 2019 Accepted: 4 September 2019 Published: 9 October 2019
Abstract
As an eminent ambassador of STEM and renowned NMR spectroscopist, Frances Separovic is an internationally famous name, but could it also be a valuable membrane-active peptide sequence? Her name has been used as an amino acid sequence (FS), successfully synthesised, oxidised, and put into contact with membrane models to investigate any serendipitous activity. The 3D structure of the cyclic FS was determined in dodecylphosphocholine (DPC) micelles by solution NMR spectroscopy. FS displayed a twisted bend separating a helical stretch and an unstructured segment. Using solid-state NMR spectroscopy, the effect of FS on 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and 1,2-dimyristoyl-sn-glycero-3-phosphoserine (DMPS) lipid bilayers was studied. FS did not strongly disturb the neutral membrane surface but likely inserted into their hydrophobic core without a strong effect on the lipid dynamics, while perturbation of the negatively charged membranes remained at the headgroup interface with a strong effect on the lipid dynamics. This study demonstrated that FS is a candidate for discovering potential future therapeutic activities.
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