ABSTRACT
Quantitative Analysis of Protein Adsorption Kinetics VLADIMIR HLADY, C.-H. HO, and D. W. BRITT Department o f Bioengineering, University of Utah, Salt Lake City, Utah
I. Protein-Surface Interactions 405 II. Methods to Study Protein Adsorption 406
III. Protein Adsorption Kinetics 407 A. Quantitative analysis o f protein adsorption B. Computation o f the flux o f protein molecules to the adsorbent
surface 407 C. Modeling o f the kinetics of lipoprotein adsorption 410
IV. Conclusions 415 List o f Symbols 417 References 417
1. PROTEIN-SURFACE INTERACTIONS
Protein adsorption from aqueous solutions is determined by the properties at two interfaces, one between the protein and the aqueous solution and the other between the adsorbent surface and the solution, and how they “match” each other. The protein-solution interface is defined by a subtle interplay between polar and nonpolar inter actions [1]. These two types of interactions govern protein stability and will also play a decisive role in protein interactions at the adsorbent surface. Other factors include the adsorbent’s surface energetics, charge, surface rugosity, and the structure of water at both interfaces, i.e., their respective hydrophilicity and interfacial hydration layers [2,3].