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Structure – membrane activity relationship in a family of peptide-based gemini amphiphiles: An insight from experimental and theoretical model systems
dc.contributor.author | Korchowiec, Beata | |
dc.contributor.author | Gorczyca, Marcelina | |
dc.contributor.author | Korchowiec, Jacek | |
dc.contributor.author | RUBIO-MAGNIETO, JENIFER | |
dc.contributor.author | Lotfallah, Ahmed H. | |
dc.contributor.author | Luis, Santiago V. | |
dc.contributor.author | Rogalska, Ewa | |
dc.coverage.spatial | Elsevier | ca_CA |
dc.date.accessioned | 2016-12-20T12:54:17Z | |
dc.date.available | 2016-12-20T12:54:17Z | |
dc.date.issued | 2016 | |
dc.identifier.issn | 0927-7765 | |
dc.identifier.issn | 1873-4367 | |
dc.identifier.uri | http://hdl.handle.net/10234/165125 | |
dc.description.abstract | A study of the interaction between five gemini amphiphilic valine-based pseudopeptides (GAPs) differing by the length of the central aliphatic spacer linking two amino acid subunits, and a model bacterial membrane lipid, 1,2-dimyristoyl-sn-glycero-3-phospho-rac-(1-glycerol) (DMPG), is here presented. Pure DMPG, pure GAPs and mixed GAPs/DMPG monolayers were formed at the air-water interface using Langmuir technique. The properties of the Langmuir films were investigated using surface pressure measurements, polarization modulation-infrared reflection-absorption spectroscopy, and Brewster angle microscopy. The atomic level information concerning the orientation of molecules in the monolayer and hydration of the polar headgroups was obtained from molecular dynamics simulations. It was demonstrated that the length of the central spacer in the GAPs structure is important for the properties of the mixed films; the disorganization of the membrane increases with the length of the spacer. The latter point is important for developing possible antimicrobial agents based on GAPs. | ca_CA |
dc.description.sponsorShip | project Interdisciplinary PhD Studies "Molecular sciences for medicine" European Social Fund within the Human Capital Operational Programme European Regional Development Fund POIG.02.01.00-12-023/08 Mineco CTQ2012-38543-C03-01 GV PROMETEO/2012/020 | ca_CA |
dc.format.extent | 9 p. | ca_CA |
dc.language.iso | eng | ca_CA |
dc.publisher | Elsevier | ca_CA |
dc.relation.isPartOf | Colloids and Surfaces B: Biointerfaces 146 (2016) 54–62 | ca_CA |
dc.rights | © 2016 Elsevier B.V. All rights reserved. | ca_CA |
dc.rights.uri | http://rightsstatements.org/vocab/InC/1.0/ | * |
dc.subject | Gemini surfactant | ca_CA |
dc.subject | Peptide | ca_CA |
dc.subject | Molecular dynamics simulations | ca_CA |
dc.subject | Biomembrane | ca_CA |
dc.title | Structure – membrane activity relationship in a family of peptide-based gemini amphiphiles: An insight from experimental and theoretical model systems | ca_CA |
dc.type | info:eu-repo/semantics/article | ca_CA |
dc.identifier.doi | http://dx.doi.org/10.1016/j.colsurfb.2016.05.040 | |
dc.rights.accessRights | info:eu-repo/semantics/restrictedAccess | ca_CA |
dc.relation.publisherVersion | http://www.sciencedirect.com/science/article/pii/S0927776516303654 | ca_CA |
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