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Synthesis and activity of a diselenide bond mimetic of the antimicrobial protein caenopore-5

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Abstract

Antimicrobial proteins are a rich source of new lead compounds for the development of new drugs that will tackle global resistance towards existing antibiotics. Caenopore-5 (Cp-5) is an antimicrobial protein (AMP) expressed in the intestine of the nematode Caenorhabditis elegans and is a member of the lipid binding saposin-like-protein family, composed of 5 α-helices and 3 disulfide bonds. Substitution of the 7Cys and 81Cys by two selenocysteine 7U and 81U afforded a selenocysteine analogue [7Sec-81Sec]-Cp-5, which displayed a higher stability (using thermal circular dichroism) compared to the native protein Cp-5. [7Sec-81Sec]-Cp-5 and an N-terminal truncated peptide exhibited cell permeability similar to the wild type Cp-5.

Graphical abstract: Synthesis and activity of a diselenide bond mimetic of the antimicrobial protein caenopore-5

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Article information


Submitted
04 Nov 2015
Accepted
06 Dec 2015
First published
07 Dec 2015

This article is Open Access
All publication charges for this article have been paid for by the Royal Society of Chemistry

Chem. Sci., 2016,7, 2005-2010
Article type
Edge Article

Synthesis and activity of a diselenide bond mimetic of the antimicrobial protein caenopore-5

K. Medini, Paul. W. R. Harris, A. Menorca, K. Hards, Gregory. M. Cook and Margaret. A. Brimble, Chem. Sci., 2016, 7, 2005
DOI: 10.1039/C5SC04187B

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