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Issue 2, 2017
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Structural features of many circular and leaderless bacteriocins are similar to those in saposins and saposin-like peptides

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Abstract

Bacteriocins are potent antimicrobial peptides that are ribosomally produced and exported by bacteria, presumably to aid elimination of competing microorganisms. Many circular and linear leaderless bacteriocins have a recuring three dimensional structural motif known as a saposin-like fold. Although these bacteriocin sizes and sequences are often quite different, and their mechanisms of action vary, this conserved motif of multiple helices appears critical for activity and may enable peptide–lipid and peptide–receptor interactions in target bacterial cell membranes. Comparisons between electrostatic surfaces and hydrophobic surface maps of different bacteriocins are discussed emphasizing similarities and differences in the context of proposed modes of action.

Graphical abstract: Structural features of many circular and leaderless bacteriocins are similar to those in saposins and saposin-like peptides

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Publication details

The article was received on 02 Nov 2016, accepted on 09 Dec 2016 and first published on 11 Jan 2017


Article type: Review Article
DOI: 10.1039/C6MD00607H
Citation: Med. Chem. Commun., 2017,8, 276-285
  • Open access: Creative Commons BY license
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    Structural features of many circular and leaderless bacteriocins are similar to those in saposins and saposin-like peptides

    K. M. Towle and J. C. Vederas, Med. Chem. Commun., 2017, 8, 276
    DOI: 10.1039/C6MD00607H

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