File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

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

TitleNanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers
Authors
KeywordsNanometrology
De novo protein design
Antibiotics
Nanoscopy
Innate host defense
Issue Date2013
Citation
Proceedings of the National Academy of Sciences of the United States of America, 2013, v. 110, n. 22, p. 8918-8923 How to Cite?
AbstractAntimicrobial 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.
Persistent Identifierhttp://hdl.handle.net/10722/301770
ISSN
2023 Impact Factor: 9.4
2023 SCImago Journal Rankings: 3.737
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorRakowska, Paulina D.-
dc.contributor.authorJiang, Haibo-
dc.contributor.authorRay, Santanu-
dc.contributor.authorPyne, Alice-
dc.contributor.authorLamarre, Baptiste-
dc.contributor.authorCarr, Matthew-
dc.contributor.authorJudge, Peter J.-
dc.contributor.authorRavi, Jascindra-
dc.contributor.authorGerling, Ulla I.M.-
dc.contributor.authorKoksch, Beate-
dc.contributor.authorMartyna, Glenn J.-
dc.contributor.authorHoogenboom, Bart W.-
dc.contributor.authorWatts, Anthony-
dc.contributor.authorCrain, Jason-
dc.contributor.authorGrovenor, Chris R.M.-
dc.contributor.authorRyadnova, Maxim G.-
dc.date.accessioned2021-08-19T02:20:42Z-
dc.date.available2021-08-19T02:20:42Z-
dc.date.issued2013-
dc.identifier.citationProceedings of the National Academy of Sciences of the United States of America, 2013, v. 110, n. 22, p. 8918-8923-
dc.identifier.issn0027-8424-
dc.identifier.urihttp://hdl.handle.net/10722/301770-
dc.description.abstractAntimicrobial 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.-
dc.languageeng-
dc.relation.ispartofProceedings of the National Academy of Sciences of the United States of America-
dc.subjectNanometrology-
dc.subjectDe novo protein design-
dc.subjectAntibiotics-
dc.subjectNanoscopy-
dc.subjectInnate host defense-
dc.titleNanoscale imaging reveals laterally expanding antimicrobial pores in lipid bilayers-
dc.typeArticle-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1073/pnas.1222824110-
dc.identifier.pmid23671080-
dc.identifier.pmcidPMC3670350-
dc.identifier.scopuseid_2-s2.0-84878432085-
dc.identifier.volume110-
dc.identifier.issue22-
dc.identifier.spage8918-
dc.identifier.epage8923-
dc.identifier.eissn1091-6490-
dc.identifier.isiWOS:000320500000050-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats