Serum albumin is the most abundant protein in blood plasma. Albumin has the ability to bind to a wide variety of compounds including drugs, and cells as well as proteins do not attach to an albumin-coated surface. These properties of albumin are attractive for biomaterials utilized in biomedical fields. In the present study, we aimed to prepare a water-insoluble albumin film possessing suitable flexibility and native albumin characteristics, such as drug binding ability and resistance to cell adhesion. To confer the film with both water insolubility and flexibility without losing albumin characteristics, we searched a suitable condition for the cross-linking of albumin. As a result, we found that a film having aimed properties could be obtained by conducting the cross-linking reaction at room temperature for 24 h using 215 mM ethylene glycol diglycidyl ether. Mouse fibroblast L929 cells did not adhere on thus obtained film in a similar manner to a native albumin-coated surface. In addition, the film could bind 2-(4'-hydroxyphenylazo)-benzoic acid, a representative albumin binding dye, and gradually release it in a pH-dependent manner.
(c) 2007 Wiley Periodicals, Inc.