Parks, people, and conservation: A review of management issues in nepal's protected areas

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/43480/1/11111_2005_Article_BF01254607.pd

Approaches to introduce helical structure in cysteine-containing peptides with a bimane group

First published: 09 June 2021An i-i+4 or i-i+3 bimane-containing linker was introduced into a peptide known to target Estrogen Receptor alpha (ERα) in order to stabilise an α-helical geometry. These macrocycles were studied by CD and NMR to reveal the i-i+4 constrained peptide adopts a 310-helical structure in solution, and an α-helical conformation on interaction with the ERα coactivator recruitment surface in silico. An acyclic bimane-modified peptide is also helical, when it includes a tryptophan or tyrosine residue; but is significantly less helical with a phenylalanine or alanine residue, which indicates such a bimane modification influences peptide structure in a sequence dependent manner. The fluorescence intensity of the bimane appears influenced by peptide conformation, where helical peptides displayed a fluorescence increase when TFE was added to phosphate buffer, compared to a decrease for less helical peptides. This study presents the bimane as a useful modification to influence peptide structure as an acyclic peptide modification, or as a side-chain constraint to give a macrocycle.Aimee J. Horsfall, Daniel P. McDougal, Denis B. Scanlon, John B. Bruning, Andrew D. Abel