Constraining cyclic peptides to mimic protein structure motifs

Hill, Timothy A., Shepherd, Nicholas E., Diness, Frederik and Fairlie, David P. (2014) Constraining cyclic peptides to mimic protein structure motifs. Angewandte Chemie (International Edition), 53 48: 13020-13041. doi:10.1002/anie.201401058

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Author Hill, Timothy A.
Shepherd, Nicholas E.
Diness, Frederik
Fairlie, David P.
Title Constraining cyclic peptides to mimic protein structure motifs
Journal name Angewandte Chemie (International Edition)   Check publisher's open access policy
ISSN 1433-7851
Publication date 2014-10-06
Sub-type Article (original research)
DOI 10.1002/anie.201401058
Volume 53
Issue 48
Start page 13020
End page 13041
Total pages 22
Place of publication Weinheim, Germany
Publisher Wiley - V C H Verlag
Language eng
Formatted abstract
Many proteins exert their biological activities through small exposed surface regions called epitopes that are folded peptides of well-defined three-dimensional structures. Short synthetic peptide sequences corresponding to these bioactive protein surfaces do not form thermodynamically stable protein-like structures in water. However, short peptides can be induced to fold into protein-like bioactive conformations (strands, helices, turns) by cyclization, in conjunction with the use of other molecular constraints, that helps to fine-tune three-dimensional structure. Such constrained cyclic peptides can have protein-like biological activities and potencies, enabling their uses as biological probes and leads to therapeutics, diagnostics and vaccines. This Review highlights examples of cyclic peptides that mimic three-dimensional structures of strand, turn or helical segments of peptides and proteins, and identifies some additional restraints incorporated into natural product cyclic peptides and synthetic macrocyclic peptidomimetics that refine peptide structure and confer biological properties.
Keyword Cyclic peptides
Natural products
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Article first published online: 6 OCT 2014

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2015 Collection
School of Chemistry and Molecular Biosciences
Institute for Molecular Bioscience - Publications
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Citation counts: TR Web of Science Citation Count  Cited 77 times in Thomson Reuters Web of Science Article | Citations
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Created: Fri, 10 Oct 2014, 20:08:23 EST by Mrs Louise Nimwegen on behalf of Institute for Molecular Bioscience