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Gemini Surfactant-Protein Interactions

2009Artigo científico Apenas metadados
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dc.contributor.authorFaustino, Celia M. C.
dc.contributor.authorCalado, Antonio R. T.
dc.contributor.authorGarcia-Rio, Luis
dc.date.accessioned2015-12-30T10:17:17Z
dc.date.available2015-12-30T10:17:17Z
dc.date.issued2009
dc.description.abstractThe interactions between bovine serum albumin (BSA) and gemini surfactants derived from cystine have been investigated and were compared with the conventional single-chain surfactant derived from cysteine. The influence of the stereochemistry of the gemini surfactant on its behavior toward BSA was also investigated, as well as the effects of pH and temperature. Electrical conductivity and surface tension measurements were used to obtain important system parameters such as critical aggregation concentration (cac), polymer saturation point (psp), degree of ionization (alpha), and the amount of surfactant binding to protein (M). Stereochemistry was found to influence the surface properties of the surfactants studied and their interaction with BSA but not their micellar properties in solution.
dc.formatapplication/pdf
dc.identifier.citationBIOMACROMOLECULES. - Vol. 10, n. 9 (SEP 2009), p. 2508-2514
dc.identifier.doihttp://dx.doi.org/10.1021/bm9004723
dc.identifier.issn1525-7797
dc.identifier.urihttp://hdl.handle.net/10451/20992
dc.language.isoeng
dc.publisherAMER CHEMICAL SOC
dc.subjectBiochemistry & Molecular Biology
dc.subjectChemistry, Organic
dc.subjectPolymer Science
dc.titleGemini Surfactant-Protein Interactions
dc.titleEffect of pH, Temperature, and Surfactant Stereochemistry
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage2514por
oaire.citation.startPage2508por
oaire.citation.titleBIOMACROMOLECULESpor
oaire.citation.volumeVol. 10por
rcaap.rightsrestrictedAccess
rcaap.typearticle

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