Serum protein adsorption and platelet adhesion on aspartic-acid-immobilized polysulfone membranes.
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.
Department of Applied Chemistry, Seikei University, 3-1 Kichijoji Kitamachi 3, Musashino, Tokyo 180-8633, Japan. higuchi@ch.seikei.ac.jp
Akon
A
Higuchi
Hirokazu
H
Hashiba
Rika
R
Hayashi
Boo Ok
BO
Yoon
Masaru
M
Sakurai
Mariko
M
Hara
D000327:Adsorption; D000328:Adult; D001224:Aspartic Acid / Q000737:chemistry*; D001798:Blood Proteins / Q000737:chemistry*; D005260:Female; D006801:Humans; D008567:Membranes, Artificial; D008855:Microscopy, Electron, Scanning; D015394:Molecular Structure; D010973:Platelet Adhesiveness; D010976:Platelet Count; D011108:Polymers / Q000737:chemistry*; D013450:Sulfones / Q000737:chemistry*; D014867:Water / Q000737:chemistry
D001798:Blood Proteins; D008567:Membranes, Artificial; D011108:Polymers; D013450:Sulfones; D014867:Water; C017662:polysulfone P 1700; D001224:Aspartic Acid