Serum protein adsorption and platelet adhesion on aspartic-acid-immobilized polysulfone membranes.

Autor: Higuchi, Akon, Hashiba, Hirokazu, Hayashi, Rika, Yoon, Boo Ok, Sakurai, Masaru, Hara, Mariko
Předmět:
Zdroj: Journal of Biomaterials Science -- Polymer Edition; Aug2004, Vol. 15 Issue 8, p1051-1063, 13p
Abstrakt: Polysulfone (PSf) membranes that covalently conjugated with aspartic acid (ASP-PSf) were prepared and analyzed for hemocompatability. Compared to PSf or other types of surface-modified PSf membranes, the ASP-PSf membranes had a reduced ability to adsorb protein from either a plasma solution or a mixed solution of albumin, globulin and fibrinogen. This appears to be due to the creation of a hydrophilic surface by the aspartic acid zwitterion immobilized on the ASP-PSf membranes. Furthermore, the analyses of membrane protein adsorption showed that a mixed protein solution recapitulates the cooperative adsorption of proteins that occurs in plasma. We also found that the number of adhering platelets was the lowest on the ASP-PSf membranes and, in general, that platelet adhesion decreased in parallel with fibrinogen adsorption. In summary, aspartic acid immobilized on the ASP-PSf membranes, which have zwitterions with a net zero charge, effectively contributes to the hydrophilic and hemocompatible sites on the surface of the hydrophobic PSf membranes. [ABSTRACT FROM AUTHOR]
Databáze: Complementary Index