Antimicrobial peptide capsids of de novo design

Emiliana Santis, Hasan Alkassem, Baptiste Lamarre, Nilofar Faruqui, Angelo Bella, James E. Noble, Nicola Micale, Santanu Ray, Jonathan R. Burns, Alexander R. Yon, Bart W. Hoogenboom and Maxim G. Ryadnov ()
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Emiliana Santis: National Physical Laboratory
Hasan Alkassem: National Physical Laboratory
Baptiste Lamarre: National Physical Laboratory
Nilofar Faruqui: National Physical Laboratory
Angelo Bella: National Physical Laboratory
James E. Noble: National Physical Laboratory
Nicola Micale: Università degli Studi di Messina
Santanu Ray: University of Brighton
Jonathan R. Burns: University College London
Alexander R. Yon: University College London
Bart W. Hoogenboom: University College London
Maxim G. Ryadnov: National Physical Laboratory

Nature Communications, 2017, vol. 8, issue 1, 1-11

Abstract: Abstract The spread of bacterial resistance to antibiotics poses the need for antimicrobial discovery. With traditional search paradigms being exhausted, approaches that are altogether different from antibiotics may offer promising and creative solutions. Here, we introduce a de novo peptide topology that—by emulating the virus architecture—assembles into discrete antimicrobial capsids. Using the combination of high-resolution and real-time imaging, we demonstrate that these artificial capsids assemble as 20-nm hollow shells that attack bacterial membranes and upon landing on phospholipid bilayers instantaneously (seconds) convert into rapidly expanding pores causing membrane lysis (minutes). The designed capsids show broad antimicrobial activities, thus executing one primary function—they destroy bacteria on contact.

Date: 2017
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DOI: 10.1038/s41467-017-02475-3

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