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Separate Molecular Determinants in Amyloidogenic and Antimicrobial Peptides

  • Michael Landreh
  • , Jan Johansson
  • , Hans Jörnvall

    Publikation: Bidrag till tidskriftArtikel i vetenskaplig tidskriftPeer review

    Sammanfattning

    Several amyloid-forming and antimicrobial peptides (AMYs and AMPs) have the ability to bind to and damage cell membranes. In addition, some AMYs possess antimicrobial activity and some AMPs form amyloid-like fibrils, relating the two peptide types and their properties. However, a comparison of their sequence characteristics reveals important differences. The high beta-strand and aggregation propensities typical of AMYs are largely absent in alpha-helix-forming AMPs, which are instead marked by a strong amphipathic moment not generally found in AMYs. Although a few peptides, for example, islet amyloid polypeptide and dermaseptin S9, combine some determinants of both groups, the structural distinctions suggest that antimicrobial activity and amyloid formation are separate features not generally associated. (C) 2014 Elsevier Ltd. All rights reserved.
    OriginalspråkEngelska
    Sidor (från-till)2159-2166
    Antal sidor8
    TidskriftJournal of Molecular Biology
    Volym426
    Nummer11
    DOI
    StatusPublicerad - 2014

    Nyckelord

    • antimicrobial peptides
    • amyloid formation
    • peptide folding
    • membrane binding
    • discordant helices

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