Spectroscopic studies of the effects of glycation of human serum albumin on L-Trp binding
Spectroscopic studies of the effects of glycation of human serum albumin on L-Trp binding
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DOI：
10.2174/092986607779117191
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发表时间：
2007-01-01
影响因子：
1.6
通讯作者：
Norouzi, Parviz
中科院分区：
文献类型：
--
作者：
Barzegar, Abolfazl;Moosavi-Movahedi, Ali A.;Norouzi, Parviz
非酶糖基化修饰蛋白质是导致糖尿病并发症发生的潜在因素之一。人血清白蛋白（HSA）是通过美拉德反应与葡萄糖相互作用的主要靶标之一。1和5毫克/毫升的葡萄糖浓度，这是一致的糖尿病患者中发现的血糖水平，对人血清白蛋白的影响进行了研究，通过圆二色性和荧光光谱在磷酸钠缓冲液，pH 7.4。HSA的部分变性和结构完整性的变化是由较低（1 mg/ml）和较高（5 mg/ml）浓度的葡萄糖的糖化引起的。为了研究结构与功能之间的关系，我们研究了L-色氨酸（L-Trp）与糖化和非糖化HSA的相互作用。结果表明，L-Trp作为基本上与HSA结合的唯一游离氨基酸，对糖化形式（特别是在低浓度葡萄糖下）的亲和力低于对非糖化HSA的亲和力。
Modification of proteins by nonenzymatic glycation is one of the underlying factors that contribute to the development of the complications of diabetes. Human serum albumin (HSA) is one of the major targets of interaction with glucose through the Maillard reaction. The effects of 1 and 5 mg/ml glucose concentrations, which are consistent with blood glucose levels found in diabetic patients, on human serum albumin were studied by circular dichroism and fluorescence spectroscopy in sodium phosphate buffer, pH 7.4. Partial denaturation and changes in the structural integrity of HSA are caused by glycation at lower (1 mg/ml) and higher (5 mg/ml) concentrations of glucose. To study the relationship between structure and function, we investigated the interaction of L-tryptophan (L-Trp) with glycated and nonglycated HSA. The results showed that L-Trp, as the only free amino acid that substantially binds to HSA, has a lower affinity for the glycated form (especially at low concentrations of glucose) than for non-glycated HSA.