Protein-surfactant interactions at hydrophobic interfaces studied with Total Internal Reflection Fluorescence Correlation Spectroscopy (TIR-FCS)
2008 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 317, no 2, 449-457 p.Article in journal (Refereed) Published
The aim of this work was to study the dynamics of proteins near solid surfaces in the presence or absence of competing surfactants by means of total internal reflection fluorescence correlation spectroscopy (TIR-FCS). Two different proteins were studied, bovine serum albumin (BSA) and Thermomyces lanuginosus lipase (TLL). A nonionic/anionic (C12E6/LAS) surfactant composition was used to mimic a detergent formulation and the surfaces used were C 18 terminated glass. It was found that with increasing surfactant concentrations the term in the autocorrelation function (ACF) representing surface binding decreased. This Suggested that the proteins were competed off the hydrophobic surface by the surfactant. When fitting the measured ACF to a model for surface kinetics, it was seen that with raised C12E6/LAS concentration, the Surface interaction rate increased for both proteins. Under these experimental conditions this meant that the time the protein was bound to the surface decreased. At 10 mu M C12E6/LAS the surface interaction was not visible for BSA, whereas it was still distinguishable in the ACF for TLL. This indicated that TLL had a higher affinity than BSA for the C 18 surface. The study showed that TIR-FCS provides a useful tool to quantify the surfactant effect on proteins adsorption.
Place, publisher, year, edition, pages
2008. Vol. 317, no 2, 449-457 p.
Hydrophobic surface; Lipase; Protein-surfactant interactions; TIR-FCS; Autocorrelation function (ACF); Hydrophobic surfaces; Protein-surfactant interactions; Total internal reflection fluorescence correlation spectroscopy (TIR-FCS); Autocorrelation; Fluorescence spectroscopy; Glass; Interfaces (materials); Lipases; Surface active agents; Proteins; bovine serum albumin; detergent; enzyme; protein; surfactant; Thermomyces lanuginosus lipase; triacylglycerol lipase; unclassified drug; adsorption; article; binding affinity; correlation function; dynamics; fluorescence analysis; hydrophobicity; kinetics; priority journal; protein interaction; spectroscopy; total internal reflection fluorescence correlation spectroscopy; Animals; Ascomycota; Binding Sites; Cattle; Fluorescent Dyes; Hydrophobicity; Lasers; Lipase; Proteins; Serum Albumin, Bovine; Spectrometry, Fluorescence; Surface Properties; Surface-Active Agents
IdentifiersURN: urn:nbn:se:kth:diva-6931DOI: 10.1016/j.jcis.2007.09.089ISI: 000251556100010ScopusID: 2-s2.0-36148937163OAI: oai:DiVA.org:kth-6931DiVA: diva2:11782
QC 20100818. Uppdaterad från Submitted till Published 20100818.2007-03-272007-03-272010-08-18Bibliographically approved