Conformations of Proteins Adsorbed at Liquid Solid Interfaces

Sylvie Noinville, Madeleine Revault

Abstract. Nonspecific adsorption of globular proteins induces conformational changes that depend upon both on the nature of the sorbent phase and on the structural stability of the protein. Because proteins can adopt various flexible three-dimensional structures under external perturbation, the surface contact with a sorbent phase can stabilise or not different conformers, which will influence the adsoprtion and desorption kinetics. Biophysical techniques such as Fourier transform infrared (FTIR) and circular dichroism spectroscopies enable the determination of the extent in secondary structures of the adsorbed protein at the aqueous-solid interface. Based on practical viewpoints of protein adsorption, we review the findings obtained in a wide range of sorbent phases such as mineral particles, colloidal systems, planar surfaces chemically modified by polymers, or self-assembled monolayers. We lay emphasis on the importance of obtaining insights into both structure and solvation during adsorption by the combined NH/ND isotope exchange and attenuated total reflectance (ATR)-FTIR techniques. We present illustrative cases of adsorption of proteins of low and high structural stabilities, bovine serum albumin and lysozyme, respectively, on either hydrophobic or hydrophilic supports.

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