Protein cleavage by transition metal complexes bearing amino acid substituents
Protein cleavage by transition metal complexes bearing amino acid substituents
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DOI：
10.1016/s0167-4838(98)00145-9
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发表时间：
1998-09-08
期刊：
影响因子：
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通讯作者：
Bocarsly, JR
中科院分区：
文献类型：
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作者：
Buranaprapuk, A;Leach, SP;Bocarsly, JR
在这份报告中，我们描述了一系列的金属配合物介导的羟基自由基的形成蛋白质损伤。使用的蛋白质靶标是牛血清白蛋白（BSA）和羧肽酶A（CPA）。BSA含有几个静电、氢键和疏水结合位点，用于与金属配合物的潜在相互作用，CPA含有特异性苯丙氨酸结合位点。本研究中提供的数据表明，所有复合物的芳香族侧链损伤和骨架断裂发生程度相似。尽管可扩散的自由基介导裂解，但可以用相对较少的识别元件获得合理水平的主链裂解特异性。引入额外的识别元件可以扩大切割位点的集合。我们表明，裂解反应的化学环境，通过使用不同的缓冲液操纵，可以显着影响裂解反应的结果。我们的工作表明，骨架切割位点由三个因素决定：金属配合物的结合位点，蛋白质骨架上的反应位点的作用，以及化学环境对反应的影响。(C)1998 Elsevier Science B.V.保留所有权利。
In this report, we describe protein damage by a series of metal complexes that mediate the formation of hydroxyl radical. The protein targets used are bovine serum albumin (BSA) and carboxypeptidase A (CPA). BSA contains several electrostatic, hydrogen bonding and hydrophobic binding sites for potential interaction with the metal complexes, and CPA contains a specific phenylalanine binding site. The data presented in this study show that aromatic side chain damage and backbone cleavage occur to similar extents with all the complexes. Reasonable levels of backbone cleavage specificity can be attained with relatively few recognition elements, despite the fact that a diffusible radical mediates cleavage. Incorporation of additional recognition elements can enlarge the set of cleavage sites. We show that the chemical environment of the cleavage reaction, manipulated by using different buffers, can dramatically affect the outcome of the cleavage reaction. Our work suggests that backbone cleavage site is determined by three factors: the binding sites of the metal complexes, the role of reactive sites on the protein backbone, and the influence of the chemical environment on the reaction. (C) 1998 Elsevier Science B.V. All rights reserved.