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Deciphering How Pore Formation Causes Strain-Induced Membrane Lysis of Lipid Vesicles Full article

Journal Journal of the American Chemical Society
ISSN: 0002-7863 , E-ISSN: 1520-5126
Output data Year: 2016, Volume: 138, Number: 4, Pages: 1406-1413 Pages count : 8 DOI: 10.1021/jacs.5b12491
Tags Peptides; Polypeptides; Pore size; Viruses
Authors Jackman Joshua A. 1 , Goh Haw Zan 1 , Zhdanov Vladimir P. 1,3 , Knoll Wolfgang 1,4 , Cho Nam-Joon 1,2
Affiliations
1 School of Materials Science and Engineering and Centre for Biomimetic Sensor Science, Nanyang Technological University, 50 Nanyang Drive 637553, Singapore
2 School of Chemical and Biomedical Engineering, Nanyang Technological University, 62 Nanyang Drive 637459, Singapore
3 Boreskov Institute of Catalysis, Russian Academy of Sciences, Novosibirsk 630090, Russia
4 Austrian Institute of Technology (AIT), Donau-City-Strasse 1, 1220 Vienna, Austria

Funding (2)

1 National Research Foundation of Singapore NRF-NRFF2011-01
2 National Medical Research Council NMRC/CBRG/0005/2012

Abstract: Pore formation by membrane-active antimicrobial peptides is a classic strategy of pathogen inactivation through disruption of membrane biochemical gradients. It remains unknown why some membrane-active peptides also inhibit enveloped viruses, which do not depend on biochemical gradients. Here, we employ a label-free biosensing approach based on simultaneous quartz crystal microbalance-dissipation and ellipsometry measurements in order to investigate how a pore-forming, virucidal peptide destabilizes lipid vesicles in a surface-based experimental configuration. A key advantage of the approach is that it enables direct kinetic measurement of the surface-bound peptide-to-lipid (P:L) ratio. Comprehensive experiments involving different bulk peptide concentrations and biologically relevant membrane compositions support a unified model that membrane lysis occurs at or above a critical P:L ratio, which is at least several-fold greater than the value corresponding to the onset of pore formation. That is consistent with peptide-induced pores causing additional membrane strain that leads to lysis of highly curved membranes. Collectively, the work presents a new model that describes how peptide-induced pores may destabilize lipid membranes through a membrane strain-related lytic process, and this knowledge has important implications for the design and application of membrane-active peptides. © 2016 American Chemical Society.
Cite: Jackman J.A. , Goh H.Z. , Zhdanov V.P. , Knoll W. , Cho N-J.
Deciphering How Pore Formation Causes Strain-Induced Membrane Lysis of Lipid Vesicles
Journal of the American Chemical Society. 2016. V.138. N4. P.1406-1413. DOI: 10.1021/jacs.5b12491 WOS Scopus РИНЦ ANCAN PMID OpenAlex
Dates:
Submitted: Dec 2, 2015
Published online: Jan 21, 2016
Published print: Feb 3, 2016
Identifiers:
Web of science: WOS:000369558000046
Scopus: 2-s2.0-84957538645
Elibrary: 26952160
Chemical Abstracts: 2016:67340
Chemical Abstracts (print): 164:196340
PMID: 26751083
OpenAlex: W2254198722
Citing:
DB Citing
Web of science 37
Scopus 37
Elibrary 35
OpenAlex 41
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