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RESEARCH ARTICLE
Contents Vol 74(9)

An Inherently Fluorescent Peptide Constraint to Define Secondary Structure: Moving Away from Auxiliary Tags

Aimee J. Horsfall https://orcid.org/0000-0003-1276-2742 A and Andrew D. Abell https://orcid.org/0000-0002-0604-2629 A B
+ Author Affiliations
- Author Affiliations

A ARC Centre of Excellence for Nanoscale Biophotonics (CNBP), The Institute for Photonics and Advanced Sensing (IPAS), Department of Chemistry, University of Adelaide, Adelaide, SA 5005, Australia.

B Corresponding author. Email: Andrew.abell@adelaide.edu.au




Aimee J. Horsfall obtained her M.Phil. (2016), and recently finalised her Ph.D. (2021) at the University of Adelaide under the supervision of Prof. Andrew D. Abell and Dr John B. Bruning. Her thesis describes techniques to study protein interactions using peptides and peptidomimetics. Aimee is now a Research Fellow at the University of Auckland with Dist. Dame Margaret Brimble and Assoc. Prof. Paul Harris.

Australian Journal of Chemistry 74(9) 686-687 https://doi.org/10.1071/CH21169
Submitted: 20 July 2021  Accepted: 16 August 2021   Published: 8 September 2021

Keywords: peptide, stapled peptide, constrained peptide, peptidomimetic, fluorescence, helical structure, bimane, secondary structure.


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