| Co-Investigator(Kenkyū-buntansha) |
OKADA Kiyotaka Kinki University, School of Medicine, Assistant Professor, 医学部, 助手 (20185432)
MATSUO Osamu Kinki University, School of Medicine, Professor, 医学部, 教授 (40030879)
SUGIYAMA Kazuo Kinki University, School of Engineering, Professor, 工学部, 教授 (00088577)
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| Budget Amount *help |
¥1,000,000 (Direct Cost: ¥1,000,000)
Fiscal Year 2003: ¥400,000 (Direct Cost: ¥400,000)
Fiscal Year 2002: ¥600,000 (Direct Cost: ¥600,000)
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| Research Abstract |
Novel polymers modified with zwitterionic L-serine or L-lysine in the side chain, poly-(O-methacryloyl-L-serine)[poly(SerMA)], poly(α-methacrylamide-L-lysine)[poly(α-LysMA)], and poly(ε-methacrylamide-L-lysine) [poly(ε-LysMA)] were prepared as a surface modifier for blood compatible biomaterials such as catheter, dialyzer and so forth, Tn this research, the evaluation of their blood compatibility has been investigated from the point of view of effects of zwitterionic polymers on the denaturation of serum proteins or platelets, on the inhibition of thrombin which plays a central role in the bloodclotting process, on the selective binding of plasminogen which is the primary zymogen in the fibrinolytic pathway, and on the enhancement of fibrinolytic activity of plasmin or plasminogen/tissue type plasminogen activator(t-PA). Poly(SerMA), poly(α-LysMA), and poly(ε-LysMA) showed the low interaction with albumin, γ-globulin, fibrinogen to prevent protein denaturation. Poly(α-LysMA) uncompetitively inhibits thrombin activity. The fibrinolytic activity by plasmin and plasminogen/t-PA, was enhanced in the presence of poly(α-LysMA) showing specific binding to plasminogen, no enhancement of their fibrinolytic activity was observed in the case of poly(SerMA) or poly(ε-LysMA). As a result ofmeasurements, it is considered that zwitterionic polymers having amino acid moiety, especially poly(α-LysMA) as a blood compatible material are applicable for use in the biomedical devices.
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