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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Bibliographic Details
Published in:Current opinion in chemical biology 2008-12, Vol.12 (6), p.692-697
Main Authors: Henchey, Laura K, Jochim, Andrea L, Arora, Paramjit S
Format: Article
Language:English
Subjects:
Animals
Cross-Linking Reagents - metabolism
Hydrogen Bonding
Models, Molecular
Peptides - chemistry
Peptides - metabolism
Protein Stability
Protein Structure, Secondary
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Summary: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.
ISSN:1367-5931
1879-0402
DOI:10.1016/j.cbpa.2008.08.019