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Titolo:
The interaction between SDS and lysozyme at the hydrophilic solid-water interface
Autore:
Green, RJ; Su, TJ; Lu, JR; Penfold, J;
Indirizzi:
Univ Surrey, Dept Chem, Guildford GU2 7XH, Surrey, England Univ Surrey Guildford Surrey England GU2 7XH ord GU2 7XH, Surrey, England IRIS, CCLRC, Didcot OX11 0QX, Oxon, England IRIS Didcot Oxon England OX110QX , CCLRC, Didcot OX11 0QX, Oxon, England
Titolo Testata:
JOURNAL OF PHYSICAL CHEMISTRY B
fascicolo: 8, volume: 105, anno: 2001,
pagine: 1594 - 1602
SICI:
1520-6106(20010301)105:8<1594:TIBSAL>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
SODIUM DODECYL-SULFATE; BOVINE SERUM-ALBUMIN; NEUTRON REFLECTION; POLY(ETHYLENE OXIDE); BETA-LACTOGLOBULIN; LIGHT-SCATTERING; ADSORPTION; PROTEINS; SURFACES; LAYERS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Lu, JR Univ Surrey, Dept Chem, Guildford GU2 7XH, Surrey, England Univ Surrey Guildford Surrey England GU2 7XH 7XH, Surrey, England
Citazione:
R.J. Green et al., "The interaction between SDS and lysozyme at the hydrophilic solid-water interface", J PHYS CH B, 105(8), 2001, pp. 1594-1602

Abstract

The interaction between sodium dodecyl sulfate (SDS) and preadsorbed lysozyme at the hydrophilic silicon oxide-water interface has been studied usingspecular neutron reflection. Measurements were carried out using two different solution concentrations of lysozyme and a range of SDS solution concentrations between 0.2 and 2 mM. The surface composition and the adsorbed layer structure were determined by varying H/D labeling of SDS. Initially, a uniform layer or bilayer of protein was formed at the interface by adsorption from either 0.03 or 1 g/L lysozyme solution concentrations. The SDS was then added to the system and the neutron reflectivity measured. It was foundthat this method of studying the SDS/lysozyme system produced highly repeatable neutron reflectivity profiles. On addition of intermediate SDS concentrations, cooperative binding of the SDS to the protein layer was observed,without any evidence of removal of the preadsorbed protein layer. On increasing the SDS concentration, to above 0.5 mM SDS, partial removal of the protein layer occurred. A concentration of 2 mM SDS was required to completely remove all traces of adsorbed material from the interface. These results suggest that the mechanism for protein elution from the interface is via the coadsorption of SDS to the protein layer and the formation of a SDS/protein complex whose surface activity varies with the extent of SDS binding.

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Documento generato il 31/03/20 alle ore 18:41:46