Johansson, Jan
- Department of Animal Biosciences, Swedish University of Agricultural Sciences
- Karolinska Institute
Research article2014Peer reviewed
Separate Molecular Determinants in Amyloidogenic and Antimicrobial Peptides
Landreh, Michael; Johansson, Jan; Jörnvall, Hans
Abstract
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.
Keywords
antimicrobial peptides; amyloid formation; peptide folding; membrane binding; discordant helices
Published in
Journal of Molecular Biology
2014, volume: 426, number: 11, pages: 2159-2166
Publisher: ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
SLU Authors
UKÄ Subject classification
Biochemistry
Molecular Biology
Biochemistry and Molecular Biology
Publication identifier
- DOI: https://doi.org/10.1016/j.jmb.2014.03.005
Permanent link to this page (URI)
https://res.slu.se/id/publ/67564