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dc.contributor.authorWasu Witoonsaridsilpen_US
dc.contributor.authorBusaba Panyarachunen_US
dc.contributor.authorNarong Sarisutaen_US
dc.contributor.authorChristel C. Müller-Goymannen_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherSrinakharinwirot Universityen_US
dc.contributor.otherTechnische Universitat Braunschweigen_US
dc.date.accessioned2018-09-24T08:48:09Z-
dc.date.available2018-09-24T08:48:09Z-
dc.date.issued2010-02-01en_US
dc.identifier.citationColloids and Surfaces B: Biointerfaces. Vol.75, No.2 (2010), 501-509en_US
dc.identifier.issn09277765en_US
dc.identifier.other2-s2.0-70549107962en_US
dc.identifier.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=70549107962&origin=inwarden_US
dc.identifier.urihttp://repository.li.mahidol.ac.th/dspace/handle/123456789/28795-
dc.description.abstractThe conformation of peptide and protein drugs in various microenvironments and the interaction with drug carriers such as liposomes are of considerable interest. In this study the influence of microenvironments such as pH, salt concentration, and surface charge on the secondary structure of a model protein, lysozyme, either in solution or entrapped in liposomes with various molar ratios of phosphatidylcholine (PC):cholesterol (Chol) was investigated. It was found that entrapment efficiency was more pronounced in negatively charged liposomes than in non-charged liposomes, which was independent of Chol content and pH of hydration medium. The occurrence of aggregation, decrease in zeta potential, and alteration of31P NMR chemical shift of negatively charged lysozyme liposomes compared to blank liposomes suggested that the electrostatic interaction plays a major role in protein-lipid binding. Addition of sodium chloride could impair the neutralizing ability of positively charged lysozyme on negatively charged membrane via chloride counterion binding. Neither lysozyme in various buffer solutions with sodium chloride nor that entrapped in liposomes showed any significant change in their secondary structures. However, significant decrease in α-helical content of lysozyme in non-charged liposomes at higher pH and salt concentrations was discovered. © 2009.en_US
dc.rightsMahidol Universityen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=70549107962&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectChemical Engineeringen_US
dc.subjectChemistryen_US
dc.subjectPhysics and Astronomyen_US
dc.titleInfluence of microenvironment and liposomal formulation on secondary structure and bilayer interaction of lysozymeen_US
dc.typeArticleen_US
dc.rights.holderSCOPUSen_US
dc.identifier.doi10.1016/j.colsurfb.2009.09.027en_US
Appears in Collections:Scopus 2006-2010

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