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Issue 3, 2016
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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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Publication details

The article was received on 04 Nov 2015, accepted on 06 Dec 2015 and first published on 07 Dec 2015


Article type: Edge Article
DOI: 10.1039/C5SC04187B
Citation: Chem. Sci., 2016,7, 2005-2010
  • Open access: Creative Commons BY license
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    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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