Frontal chromatographic analysis on dynamic behavior of protein adsorption at polymer surface

• Published in: Journal of Colloid and Interface Science Vol. 140; no. 1; pp. 66 - 74
• Main Authors: Tashiro, Yoshikazu, Kataoka, Kazunori, Sakurai, Yasuhisa
• Format: Journal Article
• Language: English; Japanese
• Published: San Diego, CA Elsevier Inc 01.11.1990; Elsevier BV; Elsevier
• Subjects: Chemistry; Exact sciences and technology; General and physical chemistry; Solid-liquid interface; Surface physical chemistry; Proteins; Frontal chromatography; Liquid solid interface; Liquid solid adsorption; Organic adsorbate; Polymer; Experimental study; Organic adsorbent
• ISSN: 0021-9797; 1095-7103
• DOI: 10.1016/0021-9797(90)90322-F

Frontal chromatography was used as a technique to examine adsorption behavior of serum proteins on polymeric biomaterials. The effect of feeding conditions, such as flow rate and concentration of protein solution loaded into column, on the adsorption mechanism is described in the present paper. The amount of bovine serum albumin and bovine immunoglobulin G (IgG) adsorbed on polystyrene was observed to be less influenced by feeding conditions, suggesting a formation of stable protein layer even in an initial stage of the adsorption due to strong hydrophobic interaction. On the other hand, the amount of adsorbed IgG on poly(2-hydroxyethyl methacrylate) (PHEMA) was increased with increasing flow rate and concentration of IgG solution loaded. This result suggests that the feeding conditions change the adsorption process of IgG, and the increase in the adsorbed amount may be explained by considering a relative difference in the rate of two consecutive processes assumed as follows: (1) adsorption of IgG to PHEMA surface, and (2) subsequent stabilization of adsorbed IgG on the surface.