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

FEBS Letters

article

Glen van den Bergen¹  Martin Stroet¹  Bertrand Caron¹  David Poger¹  Alan E. Mark¹ 

[1] School of Chemistry & Molecular Biosciences, The University of Queensland

关键词: amphipathicity;    antimicrobial peptides;    barrel-stave pores;    membrane curvature;    hydrophobic moment;    toroidal pores;   

DOI  :  10.1002/1873-3468.13705

来源: John Wiley & Sons Ltd.

【 摘 要 】

a-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 a-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/.

【 授权许可】

Unknown