Protein adsorption from human plasma is reduced on phospholipid polymers.
Protein adsorption from human plasma was investigated on phospholipid polymers, poly (2-methacryloyloxyethyl phosphorylcholine (MPC)-co-n-butyl methacrylate (BMA) or glass by radioimmunoassay and immunogold labeling techniques. In the present studies the focus was to determine the composition and distribution of proteins at the surface of these materials after contact with human blood plasma. On all materials, protein adsorption was detected and included identification of albumin, IgG, fibrinogen, fibronectin, Hageman factor (factor XII), factor VIII/von Willebrand factor, high-molecular-weight kininogen (HMWK) and the complement protein C5. The amount of protein adsorbed decreased with an increase in the MPC composition and appeared to adsorb to the surfaces in a uniform and evenly distributed manner. Therefore, we suggest that MPC moieties play an important role in suppression of protein adsorption. From these findings, it is concluded that the reduction of protein adsorption at the blood contacting surface of phospholipid polymers may result in the inhibition of thrombus formation.
Ishihara
K
K
Institute for Medical and Dental Engineering, Tokyo Medical and Dental University, Japan.
Ziats
N P
NP
Tierney
B P
BP
Nakabayashi
N
N
Anderson
J M
JM
D000327:Adsorption; D001798:Blood Proteins / Q000737:chemistry*; D006801:Humans; D007150:Immunohistochemistry; D066298:In Vitro Techniques; D007457:Iodine Radioisotopes; D008297:Male; D010743:Phospholipids / Q000737:chemistry*; D010973:Platelet Adhesiveness / Q000187:drug effects; D010974:Platelet Aggregation / Q000187:drug effects; D011108:Polymers; D011863:Radioimmunoassay; D013927:Thrombosis / Q000517:prevention & control
D001798:Blood Proteins; D007457:Iodine Radioisotopes; D010743:Phospholipids; D011108:Polymers