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|Title:||Approaches to introduce helical structure in cysteine-containing peptides with a bimane group|
|Citation:||ChemBioChem: a European journal of chemical biology, 2021; 22(17):2711-2720|
|Aimee J. Horsfall, Daniel P. McDougal, Denis B. Scanlon, John B. Bruning, Andrew D. Abell|
|Abstract:||An 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.|
|Description:||First published: 09 June 2021|
|Rights:||© 2021 Wiley-VCH GmbH|
|Appears in Collections:||Aurora harvest 8|
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