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Antimicrobial peptide capsids of de novo design
DOI:
10.1038/s41467-017-02475-3
Authors:
Emiliana
De Santis
(National Physical Laboratory)
,
Hasan
Alkassem
(National Physical Laboratory; University College London)
,
Baptiste
Lamarre
(National Physical Laboratory)
,
Nilofar
Faruqui
(National Physical Laboratory)
,
Angelo
Bella
(National Physical Laboratory, UK)
,
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)
Co-authored by industrial partner:
No
Type:
Journal Paper
Journal:
Nature Communications
, VOL 8
State:
Published (Approved)
Published:
December 2017
Diamond Proposal Number(s):
12739

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.
Journal Keywords: Antimicrobials; Protein design; Self-assembly
Subject Areas:
Biology and Bio-materials,
Medicine
Instruments:
B23-Circular Dichroism
Documents:
s41467-017-02475-3.pdf
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