Curved or linear? Predicting the 3-dimensional structure of α-helical antimicrobial peptides in an amphipathic environment.

Abstract:

:α-Helical membrane-active antimicrobial peptides (AMPs) are known to act via a range of mechanisms, including the formation of barrel-stave and toroidal pores and the micellisation of the membrane (carpet mechanism). Different mechanisms imply that the peptides adopt different 3D structures when bound at the water-membrane interface, a highly amphipathic environment. Here, an evolutionary algorithm is used to predict the 3D structure of a range of α-helical membrane-active AMPs at the water-membrane interface by optimising amphipathicity. This amphipathic structure prediction (ASP) is capable of distinguishing between curved and linear peptides solved experimentally, potentially allowing the activity and mechanism of action of different membrane-active AMPs to be predicted. The ASP algorithm is accessible via a web interface at http://atb.uq.edu.au/asp/.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

van den Bergen G,Stroet M,Caron B,Poger D,Mark AE

doi

10.1002/1873-3468.13705

subject

Has Abstract

pub_date

2020-03-01 00:00:00

pages

1062-1080

issue

6

eissn

0014-5793

issn

1873-3468

journal_volume

594

pub_type

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