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Protein epitope mimetics as anti-infectives


Robinson, J A (2011). Protein epitope mimetics as anti-infectives. Current Opinion in Chemical Biology, 15(3):379-386.

Abstract

There is growing interest in the design of synthetic molecules that mimic the structures and functions of epitopes found on the surface of peptides and proteins. Epitope mimetics can provide valuable tools to probe complex biological processes, as well as interesting leads for drug and vaccine discovery. One application of epitope mimetics is reviewed here, focusing on mimetics of the cationic antimicrobial peptides that form part of the innate immune response to microbial and viral infection in many organisms. Mimetics of these naturally occurring peptides and proteins may be useful to explore mechanisms of antimicrobial and immunomodulatory action, and as a potential source of new antibiotics to address one of the most pressing current threats to human health.

Abstract

There is growing interest in the design of synthetic molecules that mimic the structures and functions of epitopes found on the surface of peptides and proteins. Epitope mimetics can provide valuable tools to probe complex biological processes, as well as interesting leads for drug and vaccine discovery. One application of epitope mimetics is reviewed here, focusing on mimetics of the cationic antimicrobial peptides that form part of the innate immune response to microbial and viral infection in many organisms. Mimetics of these naturally occurring peptides and proteins may be useful to explore mechanisms of antimicrobial and immunomodulatory action, and as a potential source of new antibiotics to address one of the most pressing current threats to human health.

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Additional indexing

Item Type:Journal Article, refereed, further contribution
Communities & Collections:07 Faculty of Science > Department of Chemistry
Dewey Decimal Classification:540 Chemistry
Scopus Subject Areas:Physical Sciences > Analytical Chemistry
Life Sciences > Biochemistry
Language:English
Date:2011
Deposited On:09 Jan 2012 16:14
Last Modified:23 Jan 2022 20:01
Publisher:Elsevier
ISSN:1367-5931
OA Status:Green
Publisher DOI:https://doi.org/10.1016/j.cbpa.2011.02.015
PubMed ID:21419690
  • Content: Accepted Version
  • Language: English
  • Description: Full manuscript