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活化的血小板糖蛋白(GP)Ⅱ_b/Ⅲ_a复合物作为受体能识别并结合纤维蛋白原(Fg)等粘附蛋白所共有的精氨酰-甘氨酰-天冬氨酸(RGD)肽序,导致血小板聚集和血栓形成。人工合成的RGD肽段能抑制Fg与GP Ⅱb/Ⅲa结合,从而抑制血小板聚集和血栓形成。为寻找活性更高,半衰期更长的RGD肽类血小板聚集抑制剂,笔者合成了Ac-Arg-GLy-Asp-NHCH_2CH_2PR(AC-RGDPe),进行了体外抑制血小板聚集活性的评价。
The activated platelet glycoprotein (GP) II_b / III-a complex acts as an acceptor that recognizes and binds to the arginyl-glycyl-aspartic acid (RGD) peptide sequence common to adherent proteins such as fibrinogen (Fg) , Leading to platelet aggregation and thrombosis. The synthetic RGD peptide can inhibit the binding of Fg to GP Ⅱ b / Ⅲ a and thus inhibit platelet aggregation and thrombosis. In order to find a more active and longer half-life RGD peptide platelet aggregation inhibitor, the author synthesized Ac-Arg-GLy-Asp-NHCH_2CH_2PR (AC-RGDPe) and evaluated the activity of inhibiting platelet aggregation in vitro.