The University of Southampton
University of Southampton Institutional Repository

Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers

Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers
Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers

Antimicrobial peptides are postulated to disrupt microbial phospholipid membranes. The prevailing molecular model is based on the formation of stable or transient pores although the direct observation of the fundamental processes is lacking. By combining rational peptide design with topographical (atomic force microscopy) and chemical (nanoscale secondary ion mass spectrometry) imaging on the same samples, we show that pores formed by antimicrobial peptides in supported lipid bilayers are not necessarily limited to a particular diameter, nor they are transient, but can expand laterally at the nano-to-micrometer scale to the point of completemembrane disintegration. The results offer a mechanistic basis for membrane poration as a generic physicochemical process of cooperative and continuous peptide recruitment in the available phospholipidmatrix.

Antibiotics, De novo protein design, Innate host defense, Nanometrology, Nanoscopy
0027-8424
8918-8923
Rakowska, Paulina D.
73bf2145-e2fa-46ee-9ad9-f74c80d5a369
Jiang, Haibo
332f707e-1f2f-41ec-9843-dca733a1700a
Ray, Santanu
1a09c895-d9b2-472e-a358-ecbafb2cdf0e
Pyne, Alice
622be330-af77-4c54-a24f-1fbfee421957
Lamarre, Baptiste
f269271f-1c0b-4d1e-b0c3-4fd15f795bb8
Carr, Matthew
ecfdf631-8089-4f57-9a44-6bc40f412314
Judge, Peter J.
cbdf62df-bea4-49fe-8fd9-0d849ca9b528
Ravi, Jascindra
d0c93c4d-3a20-4b47-83de-588adc502509
Gerling, Ulla I.M.
bd409947-ab74-4ac6-8d6b-8907d202cd10
Koksch, Beate
94490c68-954b-48a9-bb35-0db3bb0d8ebd
Martyna, Glenn J.
20e061ee-5cc8-40db-978a-db1dc5a34c37
Hoogenboom, Bart W.
c10c1638-c55a-4363-a846-458a1514a8ff
Watts, Anthony
1aa666ad-89b7-4479-8a76-95b3aed14ce2
Crain, Jason
b68d8149-983d-4fb1-8566-aefaefc6edca
Grovenor, Chris R.M.
6d884c70-fa55-461a-b341-e1d348425807
Ryadnova, Maxim G.
0621e854-f160-40c6-ab8d-1afbf48089fd
Rakowska, Paulina D.
73bf2145-e2fa-46ee-9ad9-f74c80d5a369
Jiang, Haibo
332f707e-1f2f-41ec-9843-dca733a1700a
Ray, Santanu
1a09c895-d9b2-472e-a358-ecbafb2cdf0e
Pyne, Alice
622be330-af77-4c54-a24f-1fbfee421957
Lamarre, Baptiste
f269271f-1c0b-4d1e-b0c3-4fd15f795bb8
Carr, Matthew
ecfdf631-8089-4f57-9a44-6bc40f412314
Judge, Peter J.
cbdf62df-bea4-49fe-8fd9-0d849ca9b528
Ravi, Jascindra
d0c93c4d-3a20-4b47-83de-588adc502509
Gerling, Ulla I.M.
bd409947-ab74-4ac6-8d6b-8907d202cd10
Koksch, Beate
94490c68-954b-48a9-bb35-0db3bb0d8ebd
Martyna, Glenn J.
20e061ee-5cc8-40db-978a-db1dc5a34c37
Hoogenboom, Bart W.
c10c1638-c55a-4363-a846-458a1514a8ff
Watts, Anthony
1aa666ad-89b7-4479-8a76-95b3aed14ce2
Crain, Jason
b68d8149-983d-4fb1-8566-aefaefc6edca
Grovenor, Chris R.M.
6d884c70-fa55-461a-b341-e1d348425807
Ryadnova, Maxim G.
0621e854-f160-40c6-ab8d-1afbf48089fd

Rakowska, Paulina D., Jiang, Haibo, Ray, Santanu, Pyne, Alice, Lamarre, Baptiste, Carr, Matthew, Judge, Peter J., Ravi, Jascindra, Gerling, Ulla I.M., Koksch, Beate, Martyna, Glenn J., Hoogenboom, Bart W., Watts, Anthony, Crain, Jason, Grovenor, Chris R.M. and Ryadnova, Maxim G. (2013) Nanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers. Proceedings of the National Academy of Sciences of the United States of America, 110 (22), 8918-8923. (doi:10.1073/pnas.1222824110).

Record type: Article

Abstract

Antimicrobial peptides are postulated to disrupt microbial phospholipid membranes. The prevailing molecular model is based on the formation of stable or transient pores although the direct observation of the fundamental processes is lacking. By combining rational peptide design with topographical (atomic force microscopy) and chemical (nanoscale secondary ion mass spectrometry) imaging on the same samples, we show that pores formed by antimicrobial peptides in supported lipid bilayers are not necessarily limited to a particular diameter, nor they are transient, but can expand laterally at the nano-to-micrometer scale to the point of completemembrane disintegration. The results offer a mechanistic basis for membrane poration as a generic physicochemical process of cooperative and continuous peptide recruitment in the available phospholipidmatrix.

This record has no associated files available for download.

More information

Accepted/In Press date: 16 April 2013
Published date: 28 May 2013
Keywords: Antibiotics, De novo protein design, Innate host defense, Nanometrology, Nanoscopy

Identifiers

Local EPrints ID: 485982
URI: http://eprints.soton.ac.uk/id/eprint/485982
ISSN: 0027-8424
PURE UUID: 8093a4f8-3513-4176-8f4e-53364dab6446
ORCID for Paulina D. Rakowska: ORCID iD orcid.org/0000-0002-3710-8395

Catalogue record

Date deposited: 04 Jan 2024 18:32
Last modified: 18 Mar 2024 03:59

Export record

Altmetrics

Contributors

Author: Haibo Jiang
Author: Santanu Ray
Author: Alice Pyne
Author: Baptiste Lamarre
Author: Matthew Carr
Author: Peter J. Judge
Author: Jascindra Ravi
Author: Ulla I.M. Gerling
Author: Beate Koksch
Author: Glenn J. Martyna
Author: Bart W. Hoogenboom
Author: Anthony Watts
Author: Jason Crain
Author: Chris R.M. Grovenor
Author: Maxim G. Ryadnova

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×