Johansson, Jan
- Institutionen för husdjurens biovetenskaper, Sveriges lantbruksuniversitet
- Karolinska institutet
Forskningsartikel2014Vetenskapligt granskad
Landreh, Michael; Johansson, Jan; Jörnvall, Hans
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.
antimicrobial peptides; amyloid formation; peptide folding; membrane binding; discordant helices
Journal of Molecular Biology
2014, Volym: 426, nummer: 11, sidor: 2159-2166 Utgivare: ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
Biokemi och molekylärbiologi
DOI: https://doi.org/10.1016/j.jmb.2014.03.005
https://res.slu.se/id/publ/67564