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dc.rights.licenseopenen_US
dc.contributor.authorJOBIN, Marie-Lise
dc.contributor.authorALVES, Isabel
dc.date.accessioned2019
dc.date.available2019
dc.date.issued2019
dc.identifier.isbn978-1-4939-9178-5 978-1-4939-9179-2en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/3818
dc.description.abstractEnMembrane-active peptides include a variety of molecules such as antimicrobial (AMP), cell-penetrating (CPP), viral, and amyloid peptides that are implicated in several pathologies. They constitute important targets because they are either at the basis of novel therapies (drug delivery for CPPs or antimicrobial activity for AMPs) or they are the agents causing these pathologies (viral and amyloid peptides). They all share the common property of interacting with the cellular lipid membrane in their mode of action. Therefore, a better understanding of the peptide/lipid (P/L) interaction is essential to help decipher their mechanism of action. Among the different biophysical methods that can be used to fully characterize P/L interactions, differential scanning calorimetry (DSC) allows determining the peptide effect on the lipid phase transitions, a property that reflects the P/L interaction mode. A general protocol for classical DSC experiments for P/L studies will be provided.
dc.language.isoENen_US
dc.publisherHumana Pressen_US
dc.publisher.locationNew Yorken_US
dc.source.titleMethods in Molecular Biologyen_US
dc.subject.enMembrane-active peptides
dc.subject.enPeptide/lipid interaction
dc.subject.enDifferential scanning calorimetry
dc.subject.enLipid phase transition
dc.subject.enThermodynamic behavior
dc.title.enThe Contribution of Differential Scanning Calorimetry for the Study of Peptide/Lipid Interactions
dc.typeChapitre d'ouvrageen_US
dc.identifier.doi10.1007/978-1-4939-9179-2_1
dc.subject.halChimie/Matériauxen_US
bordeaux.page3-15en_US
bordeaux.volume1964en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.inpressnonen_US
hal.identifierhal-03160304
hal.version1
hal.date.transferred2021-03-05T09:01:25Z
hal.exporttrue
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