ADSA-TRIS: a new method to study interfacial phenomena at polymer-aqueous solution interfaces
Axisymmetric drop shape analysis-profile (ADSA-P) was combined with total reflectometric interference spectroscopy (TRIS) in one experimental setup to study the interfacial phenomena at solid-liquid and liquid-vapor interfaces caused by adsorption/desorption (dissolution) of surface-active substance...
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Veröffentlicht in: | Analytical and bioanalytical chemistry 2008-07, Vol.391 (5), p.1739-1749 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Axisymmetric drop shape analysis-profile (ADSA-P) was combined with total reflectometric interference spectroscopy (TRIS) in one experimental setup to study the interfacial phenomena at solid-liquid and liquid-vapor interfaces caused by adsorption/desorption (dissolution) of surface-active substances. Using sessile liquid droplets on polymer film/chromium-coated glass substrates that were optically matched with an immersion oil to a TRIS reflection prism, the optical thickness (product of physical thickness d and refractive index n) of the polymer film can be estimated by evaluating the wavelength-dependent intensity of reflected light. The sessile droplet is analyzed simultaneously by an ADSA setup arranged in a transverse direction to the path of the white-light beam of TRIS. From this analysis, the solid-vapor interfacial tension γ lv(t), contact angle θ(t), contact radius r(t), drop volume V(t), and solid-liquid interfacial tension γ sl(t) can be monitored as a function of time. The new method was applied to study polystyrene and poly(4-hydroxystyrene) surfaces in contact with aqueous buffer solutions and with protein solutions. The time-dependent changes in the optical film thickness caused by the adsorption of human serum albumin (HSA) and lysozyme (LSZ) were accompanied by changes in the solid-liquid interfacial tension. From the detailed study of both parameters, conclusions can be drawn with regard to the adsorption kinetics of the proteins on the hydrophobic polystyrene surfaces and to conformational changes occurring within the adsorbed protein layers. [graphic removed] |
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ISSN: | 1618-2642 1618-2650 |
DOI: | 10.1007/s00216-007-1816-8 |