Format

Send to:

Choose Destination
See comment in PubMed Commons below
Curr Opin Chem Biol. 2008 Dec;12(6):692-7. doi: 10.1016/j.cbpa.2008.08.019. Epub 2008 Sep 13.

Contemporary strategies for the stabilization of peptides in the alpha-helical conformation.

Author information

  • 1Department of Chemistry, New York University, 100 Washington Square East, New York, NY 10003, USA.

Abstract

Herein we review contemporary synthetic and protein design strategies to stabilize the alpha-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 alpha-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.

PMID:
18793750
[PubMed - indexed for MEDLINE]
PMCID:
PMC2650020
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Write to the Help Desk