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dc.contributor.authorMcauley, William J.
dc.contributor.authorJones, David S.
dc.contributor.authorKett, Vicky L.
dc.date.accessioned2013-01-11T14:29:10Z
dc.date.available2013-01-11T14:29:10Z
dc.date.issued2009-08
dc.identifier.citationMcauley , W J , Jones , D S & Kett , V L 2009 , ' Characterisation of the Interaction of Lactate Dehydrogenase With Tween-20 Using Isothermal Titration Calorimetry, Interfacial Rheometry and Surface Tension Measurements ' Journal of Pharmaceutical Sciences , vol 98 , no. 8 , pp. 2659-2669 . , 10.1002/jps.21640en
dc.identifier.issn0022-3549
dc.identifier.otherPURE: 437906
dc.identifier.otherPURE UUID: 5ca7e6a1-9d6c-4a01-876d-53d9eca8295e
dc.identifier.otherWOS: 000268600300010
dc.identifier.urihttp://hdl.handle.net/2299/9587
dc.descriptionFull text of this item is not available in the UHRAen
dc.description.abstractIn this study the nature of the interaction between Tween-20 and lactate dehydrogenase (LDH) was investigated using isothermal titration calorimetry (ITC). In addition the effects of the protein and surfactant on the interfacial properties were followed with interfacial rheology and surface tension measurements in order to understand the mechanism by which the surfactant prevents protein adsorption to the air-water interface. Comparisons were made with Tween-40 and Tween-80 in order to further investigate the mechanism. ITC measurements indicated a weak, probably hydrophobic, interaction between Tween-20 and LDH. Prevention of LDH adsorption to the air-water interface by the Tween surfactants was correlated with Surface energy rather than surfactant CMC. While surface pressure appears to be the main driving force for the displacement of LDH from the air-water interface by Tween-20 a solubilisation mechanism may exist for other protein molecules. More generally the results of this study highlight the value of the use of ITC and interfacial measurements in characterising the surface behaviour of mixed surfactant and protein systems. (C) 2009 Wiley-Liss, Inc. and the American Pharmacists Association J Pharm Sci 98:2659-2669, 2009en
dc.format.extent11en
dc.language.isoeng
dc.relation.ispartofJournal of Pharmaceutical Sciencesen
dc.subjectproteinsen
dc.subjectnon-ionic surfactantsen
dc.subjectsurface tensionen
dc.subjectinterfacial rheologyen
dc.subjectisothermal titration calorimetryen
dc.subjecthydrophobic interactionsen
dc.subjectBOVINE SERUM-ALBUMINen
dc.subjectHUMAN GROWTH-HORMONEen
dc.subjectAIR-WATER-INTERFACEen
dc.subjectBETA-LACTOGLOBULINen
dc.subjectGLOBULAR-PROTEINSen
dc.subjectMODEL PROTEINen
dc.subjectRECOMBINANTen
dc.subjectADSORPTIONen
dc.subjectLAYERSen
dc.subjectSTABILIZATIONen
dc.titleCharacterisation of the Interaction of Lactate Dehydrogenase With Tween-20 Using Isothermal Titration Calorimetry, Interfacial Rheometry and Surface Tension Measurementsen
dc.typeArticleen
dc.contributor.institutionDepartment of Pharmacyen
dc.contributor.institutionSchool of Life and Medical Sciencesen
dc.contributor.institutionHealth & Human Sciences Research Instituteen
dc.contributor.institutionCentre for Research into Topical Drug Delivery and Toxicologyen
dc.contributor.institutionPharmaceuticsen
dc.contributor.institutionSkin and Nail Groupen
dc.contributor.institutionPharmaceutical Analysis and Product Characterisationen
dc.identifier.doihttp://dx.doi.org/10.1002/jps.21640
dc.description.statusPeer revieweden
dc.relation.schoolSchool of Life and Medical Sciences
herts.preservation.rarelyaccessedtrue


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