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 Lettjournal_title
FEBS lettersauthors
van den Bergen G,Stroet M,Caron B,Poger D,Mark AEdoi
10.1002/1873-3468.13705subject
Has Abstractpub_date
2020-03-01 00:00:00pages
1062-1080issue
6eissn
0014-5793issn
1873-3468journal_volume
594pub_type
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