Mid Sweden University

miun.sePublications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
The Importance of Cyclic Structure for Labaditin on Its Antimicrobial Activity Against Staphylococcus aureus
Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos, SP, Brazil.
Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos, SP, Brazil.
Mid Sweden University, Faculty of Science, Technology and Media, Department of Natural Sciences.
Departamento de Química, Faculdade de Filosofia, Ciências e Letras de Ribeirão Preto, Universidade de São Paulo, Ribeirão Preto, SP, Brazil.
Show others and affiliations
2016 (English)In: Colloids and Surfaces B: Biointerfaces, ISSN 0927-7765, E-ISSN 1873-4367, Vol. 148, p. 453-459Article in journal (Refereed) Published
Abstract [en]

Antimicrobial resistance has reached alarming levels in many countries, thus leading to a search for new classes of antibiotics, such as antimicrobial peptides whose activity is exerted by interacting specifically with the microorganism membrane. In this study, we investigate the molecular-level mechanism of action for Labaditin (Lo), a 10-amino acid residue cyclic peptide from Jatropha multifida with known bactericidal activity againstStreptococcus mutans. We show that Lo is also effective against Staphylococcus aureus(S. aureus) but this does not apply to its linear analogue (L1). Using polarization-modulated infrared reflection absorption spectroscopy (PM-IRRAS), we observed with that the secondary structure of Lo was preserved upon interacting with Langmuir monolayers from a phospholipid mixture mimicking S. aureus membrane, in contrast to L1. This structure preservation for the rigid, cyclic Lo is key for the self-assembly of peptide nanotubes that induce pore formation in large unilamellar vesicles (LUVs), according to permeability assays and dynamic light scattering measurements. In summary, the comparison between Labaditin (Lo) and its linear analogue L1 allowed us to infer that the bactericidal activity of Lo is more related to its interaction with the membrane. It does not require specific metabolic targets, which makes cyclic peptides promising for antibiotics without bacteria resistance.

Place, publisher, year, edition, pages
2016. Vol. 148, p. 453-459
Keywords [en]
Antimicrobial peptide, Cyclic peptides, Labaditin, Langmuir monolayers, Large unilamellar vesicles, Peptide nanotubes, PM-IRRAS, Staphylococcus aureus
National Category
Physical Sciences
Identifiers
URN: urn:nbn:se:miun:diva-28955DOI: 10.1016/j.colsurfb.2016.09.017ISI: 000388248500051PubMedID: 27665378Scopus ID: 2-s2.0-84988644078OAI: oai:DiVA.org:miun-28955DiVA, id: diva2:974756
Available from: 2016-09-27 Created: 2016-09-27 Last updated: 2017-11-21Bibliographically approved

Open Access in DiVA

No full text in DiVA

Other links

Publisher's full textPubMedScopus

Authority records

Volpati, Diogo

Search in DiVA

By author/editor
Volpati, Diogo
By organisation
Department of Natural Sciences
In the same journal
Colloids and Surfaces B: Biointerfaces
Physical Sciences

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 252 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf