The role of electrolytes on protein adsorption at a hydrophilic solid-water interface.
The adsorption of four proteins, RNase A, HEWL, BSA, and beta-Lac, was examined on the surface of a negatively charged SiO(2)/TiO(2) optical waveguide. The amount of adsorbed protein followed the salt series Mg(2+)>Li(+)>Na(+)>K(+) and for anions Cl(-)>Br(-)>I(-). This ordering was attributed to protein adsorption being primarily influenced by changes in hydrophobic interactions between the surface and the protein resulting from differences in water structure arising from the presence of electrolytes.
Wendorf
Janet R
JR
Department of Chemical Engineering, University of California, Berkeley, 491 Tan Hall, Berkeley, CA 94720-1462, USA.
Radke
Clayton J
CJ
Blanch
Harvey W
HW
D000327:Adsorption / Q000187:drug effects; D000818:Animals; D000838:Anions / Q000737:chemistry; D002021:Buffers; D002412:Cations / Q000737:chemistry; D002417:Cattle; D002645:Chickens; D004573:Electrolytes / Q000737:chemistry*; D006863:Hydrogen-Ion Concentration / Q000187:drug effects; D057927:Hydrophobic and Hydrophilic Interactions; D007782:Lactoglobulins / Q000378:metabolism; D008956:Models, Chemical; D009113:Muramidase / Q000378:metabolism; D011506:Proteins / Q000378:metabolism*; D012259:Ribonuclease, Pancreatic / Q000378:metabolism; D012710:Serum Albumin, Bovine / Q000378:metabolism; D012965:Sodium Chloride / Q000494:pharmacology; D012996:Solutions; D013499:Surface Properties / Q000187:drug effects; D014867:Water / Q000737:chemistry*
D000838:Anions; D002021:Buffers; D002412:Cations; D004573:Electrolytes; D007782:Lactoglobulins; D011506:Proteins; D012996:Solutions; D014867:Water; D012710:Serum Albumin, Bovine; D012965:Sodium Chloride; D012259:Ribonuclease, Pancreatic; C421864:hen egg lysozyme; D009113:Muramidase