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

Akon Higuchi, Hirokazu Hashiba, Rika Hayashi, Boo Ok Yoon, Masaru Sakurai, Mariko Hara

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)1051-1063
Number of pages13
JournalJournal of Biomaterials Science, Polymer Edition
Volume15
Issue number8
DOIs
StatePublished - 2004

Keywords

  • Blood compatibility
  • Membrane
  • Polysulfone
  • Protein adsorption
  • Surface modification
  • Zwitterion

Fingerprint

Dive into the research topics of 'Serum protein adsorption and platelet adhesion on aspartic-acid-immobilized polysulfone membranes'. Together they form a unique fingerprint.

Cite this