title: Selective adsorption of protein molecules on phase-separated sapphire surfaces.
abstract: Site-selective adsorption of protein molecules was found on sapphire surfaces that exhibit a phase separation into two domains: weakly charged hydrophobic domain and negatively charged hydrophilic one. Ferritin and bovine serum albumin molecules, which are negatively charged in a buffer solution, are adsorbed to the hydrophobic domains. Avidin molecules, which are positively charged, are adsorbed to the other domain. Fibrinogen molecules, which consist of both negative and positive modules, are adsorbed to the whole sapphire surface. Hemoglobin molecules, whose net charge is almost zero, are also adsorbed to the whole surfaces. These results indicate that electrostatic double layer interaction is the primary origin of the observed selectivity. Dependence of protein adsorption or desorption behaviors on the pH value can also be interpreted by the proposed model.
authors.affiliation: Yokohama National University, Hodogaya, Yokohama, Japan.
authors.forename: Kenji
authors.initials: K
authors.lastname: Yamazaki
authors.forename: Takayuki
authors.initials: T
authors.lastname: Ikeda
authors.forename: Toshinari
authors.initials: T
authors.lastname: Isono
authors.forename: Toshio
authors.initials: T
authors.lastname: Ogino
mesh_terms: D000327:Adsorption; D000537:Aluminum Oxide / Q000737:chemistry*; D000818:Animals; D001360:Avidin / Q000302:isolation & purification; D002417:Cattle; D005293:Ferritins / Q000302:isolation & purification; D005340:Fibrinogen / Q000302:isolation & purification; D006736:Horses; D006863:Hydrogen-Ion Concentration; D011506:Proteins / Q000302:isolation & purification*; D012710:Serum Albumin, Bovine / Q000302:isolation & purification; D013499:Surface Properties
chemical_list: D011506:Proteins; D001360:Avidin; D012710:Serum Albumin, Bovine; D005340:Fibrinogen; D005293:Ferritins; D000537:Aluminum Oxide