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Micelle density regulated by a reversible switch of protein secondary structure

dc.rights.licenseopen
hal.structure.identifierDepartment of Biomedical Engineering [Atlanta]
dc.contributor.authorSALLACH, Rory E.
hal.structure.identifierEmory Univ, Dept Surg
dc.contributor.authorWEI, Min
hal.structure.identifierUniv Georgia, Dept Chem
dc.contributor.authorBISWAS, Nilanjana
hal.structure.identifierEmory Univ, Dept Chem
dc.contributor.authorCONTICELLO, Vincent P.
hal.structure.identifierLaboratoire de Chimie des polymères organiques [LCPO]
hal.structure.identifierTeam 3 LCPO : Polymer Self-Assembly & Life Sciences
dc.contributor.authorLECOMMANDOUX, Sebastien
hal.structure.identifierUniv Georgia, Dept Chem
dc.contributor.authorDLUHY, Richard A.
hal.structure.identifierDepartment of Biomedical Engineering [Atlanta]
hal.structure.identifierLab Biomol Mat Res [Emory Univ]
hal.structure.identifierGeorgia Inst Technol, Sch Chem & Biomol Engn
dc.contributor.authorCHAIKOF, Elliot L.
dc.date.accessioned2020
dc.date.available2020
dc.date.issued2006
dc.identifier.issn0002-7863
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/20726
dc.description.abstractEnProtein secondary structures may exhibit reversible transitions that occur in an abrupt and controllable manner. In this report, we demonstrate that such transitions may be utilized in the design of a "smart" protein micellar system, in which a stimulus-induced change in protein structure triggers a rapid change in micelle compacticity and size. Specifically, recombinant DNA methods were used to prepare a protein triblock copolymer containing a central hydrophilic block and two hydrophobic end blocks derived from elastin-mimetic peptide sequences. Below the copolymer inverse transition temperature (T-t), dilute solutions of this amphiphilic protein formed monodispersed micelles in a narrow range of R-H of similar to 100 nm. When the the temperature was raised above T-t, an abrupt increase in micelle internal density was observed with a concomitant reduction in micelle size. This reversible change in micelle compacticity was triggered by helix-to-sheet protein folding transition. Significantly, these protein polymer-based micelles, which are rapidly responsive to environmental stimuli, establish a new mechanism for the design of controlled drug delivery vehicles.
dc.language.isoen
dc.publisherAmerican Chemical Society
dc.subject.encopolymer
dc.subject.enconformation
dc.subject.enbeta-sheet
dc.subject.enelastin
dc.subject.eninverse temperature transition
dc.subject.enLCST
dc.subject.enprotein
dc.subject.enalpha-helix
dc.title.enMicelle density regulated by a reversible switch of protein secondary structure
dc.typeArticle de revue
dc.identifier.doi10.1021/ja0638509
dc.subject.halChimie/Polymères
bordeaux.journalJournal of the American Chemical Society
bordeaux.page12014-12019
bordeaux.volume128
bordeaux.hal.laboratoriesLaboratoire de Chimie des Polymères Organiques (LCPO) - UMR 5629*
bordeaux.issue36
bordeaux.institutionBordeaux INP
bordeaux.institutionUniversité de Bordeaux
bordeaux.peerReviewedoui
hal.identifierhal-00369216
hal.version1
hal.origin.linkhttps://hal.archives-ouvertes.fr//hal-00369216v1
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