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Contemporary strategies for the stabilization of peptides in the α-helical conformation
Herein we review contemporary synthetic and protein design strategies to stabilize the α-helical motif in short peptides and miniature proteins. Advances in organometallic catalyst design, specifically for the olefin metathesis reaction, enable the use of hydrocarbon bridges to either crosslink side...
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Published in: | Current opinion in chemical biology 2008-12, Vol.12 (6), p.692-697 |
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container_title | Current opinion in chemical biology |
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creator | Henchey, Laura K Jochim, Andrea L Arora, Paramjit S |
description | Herein we review contemporary synthetic and protein design strategies to stabilize the α-helical motif in short peptides and miniature proteins. Advances in organometallic catalyst design, specifically for the olefin metathesis reaction, enable the use of hydrocarbon bridges to either crosslink side chains of specific residues or mimic intramolecular hydrogen bonds with carbon–carbon bonds. The resulting hydrocarbon-stapled and hydrogen bond surrogate α-helices provide unique synthetic ligands for targeting biomolecules. In the protein design realm, several classes of miniature proteins that display stable helical domains have been engineered and manipulated with powerful
in vitro selection technologies to yield libraries of sequences that retain their helical folds. Rational re-design of these scaffolds provide distinctive reagents for the modulation of protein–protein interactions. |
doi_str_mv | 10.1016/j.cbpa.2008.08.019 |
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subjects | Animals Cross-Linking Reagents - metabolism Hydrogen Bonding Models, Molecular Peptides - chemistry Peptides - metabolism Protein Stability Protein Structure, Secondary |
title | Contemporary strategies for the stabilization of peptides in the α-helical conformation |
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