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Antimicrobial peptide capsids of de novo design
by
Faruqui, Nilofar
, Yon, Alexander R.
, De Santis, Emiliana
, Burns, Jonathan R.
, Bella, Angelo
, Micale, Nicola
, Hoogenboom, Bart W.
, Ray, Santanu
, Alkassem, Hasan
, Ryadnov, Maxim G.
, Noble, James E.
, Lamarre, Baptiste
in
101/28
/ 14/19
/ 14/3
/ 631/1647/338/22
/ 631/92/469
/ 639/638/541/966
/ Anti-Infective Agents - chemical synthesis
/ Anti-Infective Agents - metabolism
/ Anti-Infective Agents - pharmacology
/ Antibiotics
/ Antiinfectives and antibacterials
/ Antimicrobial agents
/ Antimicrobial Cationic Peptides - chemical synthesis
/ Antimicrobial Cationic Peptides - metabolism
/ Antimicrobial Cationic Peptides - pharmacology
/ Bacteria
/ Bacteria - drug effects
/ Capsid - metabolism
/ Capsid - ultrastructure
/ Capsids
/ Chemistry Techniques, Synthetic - methods
/ Chromatography, High Pressure Liquid
/ Cryoelectron Microscopy
/ Drug Discovery
/ Drug Resistance, Bacterial
/ Humanities and Social Sciences
/ Humans
/ Image resolution
/ Lipid Bilayers - metabolism
/ Lysis
/ Microbial Sensitivity Tests
/ Microscopy, Electron, Transmission
/ multidisciplinary
/ Phospholipids
/ Science
/ Science (multidisciplinary)
/ Shells
/ Topology
/ Viruses
2017
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Antimicrobial peptide capsids of de novo design
by
Faruqui, Nilofar
, Yon, Alexander R.
, De Santis, Emiliana
, Burns, Jonathan R.
, Bella, Angelo
, Micale, Nicola
, Hoogenboom, Bart W.
, Ray, Santanu
, Alkassem, Hasan
, Ryadnov, Maxim G.
, Noble, James E.
, Lamarre, Baptiste
in
101/28
/ 14/19
/ 14/3
/ 631/1647/338/22
/ 631/92/469
/ 639/638/541/966
/ Anti-Infective Agents - chemical synthesis
/ Anti-Infective Agents - metabolism
/ Anti-Infective Agents - pharmacology
/ Antibiotics
/ Antiinfectives and antibacterials
/ Antimicrobial agents
/ Antimicrobial Cationic Peptides - chemical synthesis
/ Antimicrobial Cationic Peptides - metabolism
/ Antimicrobial Cationic Peptides - pharmacology
/ Bacteria
/ Bacteria - drug effects
/ Capsid - metabolism
/ Capsid - ultrastructure
/ Capsids
/ Chemistry Techniques, Synthetic - methods
/ Chromatography, High Pressure Liquid
/ Cryoelectron Microscopy
/ Drug Discovery
/ Drug Resistance, Bacterial
/ Humanities and Social Sciences
/ Humans
/ Image resolution
/ Lipid Bilayers - metabolism
/ Lysis
/ Microbial Sensitivity Tests
/ Microscopy, Electron, Transmission
/ multidisciplinary
/ Phospholipids
/ Science
/ Science (multidisciplinary)
/ Shells
/ Topology
/ Viruses
2017
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Antimicrobial peptide capsids of de novo design
by
Faruqui, Nilofar
, Yon, Alexander R.
, De Santis, Emiliana
, Burns, Jonathan R.
, Bella, Angelo
, Micale, Nicola
, Hoogenboom, Bart W.
, Ray, Santanu
, Alkassem, Hasan
, Ryadnov, Maxim G.
, Noble, James E.
, Lamarre, Baptiste
in
101/28
/ 14/19
/ 14/3
/ 631/1647/338/22
/ 631/92/469
/ 639/638/541/966
/ Anti-Infective Agents - chemical synthesis
/ Anti-Infective Agents - metabolism
/ Anti-Infective Agents - pharmacology
/ Antibiotics
/ Antiinfectives and antibacterials
/ Antimicrobial agents
/ Antimicrobial Cationic Peptides - chemical synthesis
/ Antimicrobial Cationic Peptides - metabolism
/ Antimicrobial Cationic Peptides - pharmacology
/ Bacteria
/ Bacteria - drug effects
/ Capsid - metabolism
/ Capsid - ultrastructure
/ Capsids
/ Chemistry Techniques, Synthetic - methods
/ Chromatography, High Pressure Liquid
/ Cryoelectron Microscopy
/ Drug Discovery
/ Drug Resistance, Bacterial
/ Humanities and Social Sciences
/ Humans
/ Image resolution
/ Lipid Bilayers - metabolism
/ Lysis
/ Microbial Sensitivity Tests
/ Microscopy, Electron, Transmission
/ multidisciplinary
/ Phospholipids
/ Science
/ Science (multidisciplinary)
/ Shells
/ Topology
/ Viruses
2017
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Journal Article
Antimicrobial peptide capsids of de novo design
2017
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Overview
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.
With the growing threat of antibiotic resistance, unconventional approaches to antimicrobial discovery are needed. Here, the authors present a peptide topology that mimics virus architecture and assembles into antimicrobial capsids that disrupt bacterial membranes upon contact.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 14/19
/ 14/3
/ Anti-Infective Agents - chemical synthesis
/ Anti-Infective Agents - metabolism
/ Anti-Infective Agents - pharmacology
/ Antiinfectives and antibacterials
/ Antimicrobial Cationic Peptides - chemical synthesis
/ Antimicrobial Cationic Peptides - metabolism
/ Antimicrobial Cationic Peptides - pharmacology
/ Bacteria
/ Capsids
/ Chemistry Techniques, Synthetic - methods
/ Chromatography, High Pressure Liquid
/ Humanities and Social Sciences
/ Humans
/ Lysis
/ Microscopy, Electron, Transmission
/ Science
/ Shells
/ Topology
/ Viruses
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