Polymer(Korea), Vol.5, No.6, 459-466, December, 1981
Polypeptide의 구조와 항혈전성
Conformation and Thromboresistance of Polypeptides
초록
Glycine(Gly), alanine(Ala), proline(Pro), 및 γ-benzyl-L-glutamate(γ-BLG)를 서로 공중합하여 얻은 copolypeptide의 항혈전성을 검토하였다. 항혈전성에 영향을 미치는 인자는 임계표면장력(γc) 및 혈액응고시간(C.T.)을 측정하였다. 접촉각측정으로부터 임계표면장력을 구한 결과, Gly-Ala공중합체에서는 α-helix함량이 증가할수록 γc은 증가하나, β-구조함량이 증가하면 γc은 감소한다. 혈액적합성을 검토하기 위하여 Lee-White법으로 혈액응고시간을 측정한 결과, Ala-Pro copolypeptide의 경우 고유광회전도가 감소하면 C.T.은 감소하고, Proline의 함량이 증가할수록 C.T.가 감소하고 있다. 이것은 팹티드결합중에서 수소결합을 하지 않은 카르보닐기에 의한 혈장단백질의 흡착때문으로 생각된다. Gly-γ-BLG copolypeptide에서 glycine함량이 증가할수록 C.T.가 증가하는 반면, γc은 감소하고 있어, γc와 C.T.은 서로 반비례하고 있다. 즉 이것은 임계표면장력이 낮은 소수성표면이 항혈전성에 좋다는 것을 나타내는 결과이다.
The thromboresistance of some copolypeptides prepared from four amino acids, glycine(Gly), alanine(Ala), proline(Pro) and γ-benzyl-L-glutamate (γBLG), was investigated. The influencing factors on thromboresistance such as critical surface tension (γc) and clotting time were measured. In Gly-Ala copolypeptide, γc determined from the contact angle measurements was found to increase as the α-helical content increased. To examine the blood compatibility of the copolypeptides clotting time determined according to the Lee-White methods decreased with decreasing optical rotatory dispersion, and with the increase in proline content in Ala-Procopolypeptides. This decrease was thought to result from the adsorption of plasma protein to carbonyl bond which doesn''t have hydrogen bond in poly-L-proline. In Gly-γBLG copolymer clotting time was found to increase as the glycine content increased, whereas critical surface tension increased as the γBLG content increased. Discussions of the influence of hydrophobicity on the thromboresistance was made.