HYDROGEN-BONDS BETWEEN PROTEIN SIDE-CHAINS AND PHOSPHATES AND THEIR ROLE IN BIOLOGICAL CALCIFICATION
HYDROGEN-BONDS BETWEEN PROTEIN SIDE-CHAINS AND PHOSPHATES AND THEIR ROLE IN BIOLOGICAL CALCIFICATION
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DOI：
10.1016/0301-4622(87)80085-6
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发表时间：
1987-11-01
影响因子：
3.8
通讯作者：
RODRIGUEZ, ML
中科院分区：
文献类型：
--
作者：
CARMONA, P;RODRIGUEZ, ML
用红外光谱法研究了Ca2+存在下聚l -组氨酸-磷酸（H2PO4-, HPO42-）和聚l -谷氨酸-磷酸（残磷酸盐，1:1）体系。在聚l -组氨酸-磷酸体系中，N…跳.dblarw。NH +……O-P氢键是在组氨酸环上发现大多数磷酸质子的地方形成的。随着水化程度的增加，质子限制结构NH+的比例增加。O-P增加。在聚谷氨酸-磷酸二氢体系中，大多数磷酸质子位于羧酸基上。在聚谷氨酸-磷酸氢混合物中观察到不同的行为，其中磷酸质子在氢受体羧酸基上的停留时间非常短。然而，这种停留时间随着湿度的增加而增加。所有这些结果都支持生物钙化的三相理论，涉及到一个三方蛋白质-钙-磷酸复合物，其中这些氢键可以存在。这些氢键的行为也可以解释在含草酸钙的尿路结石中形成磷酸钙病灶的原因。
Poly(L-histidine)-phosphate (H2PO4-, HPO42-) and poly(L-glutamate)-phosphate systems (residue phosphate, 1 : 1) in the presence of Ca2+ ae studied by infrared spectroscopy. In the poly(L-histidine)-phosphate systems N...HOP .dblarw. NH+... O-P hydrogen bonds are formed where most phosphate protons are found at the histidine ring. With an increase in the degree of hydration the proportion of the proton limiting structure NH+...O-P increases. In the poly(L-glutamate)-dihydrogen phosphate system most phosphate protons are found at the carboxylate groups. Different behavior is observed for poly(L-glutamate)-hydrogen phosphate mixtures, where the residence time of the phosphate proton at the hydrogen acceptor carboxylate group is very short. This residence time increases, however, with increasing humidity. All these results support the triphasic theory of biological calcification involving a tripartite protein-calcium-phosphate complex where these hydrogen bonds can be present. The behavior of these hydrogen bonds can also explain the formation of a nidus of calcium phosphate salt in calcium oxalate-containing urinary calculi.