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首页> 外文期刊>Dalton transactions: An international journal of inorganic chemistry >Binding of Ni2+ and Cu2+ ions to peptides with a Cys-His motif
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Binding of Ni2+ and Cu2+ ions to peptides with a Cys-His motif

机译:Ni2 +和Cu2 +离子与具有Cys-His基序的肽结合

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摘要

Waglerin I is a 22 amino acid snake venom toxin. Its three fragments (GGKPDLRPCHP-NH2, PCHYIPRPKPR-NH2, PCHPPCHYIPR-NH2), due to the presence of two Cys and His residues, are potentially very attractive ligands for transition metal ions. The main aim of this work was to establish the impact of these two adjacent residues on Ni2+ ion binding, especially because this kind of motif is very common in nature, and the study of low molecular weight models could be helpful in understanding larger systems. In this work waglerin fragments and their N-protected analogues were studied with Ni2+ (and Cu2+ for peptides with disulfide bridges) ions using combined potentiometric and spectroscopic measurements (UV-Vis, CD, EPR and NMR). In all peptides, except PCHPPCHYIPR-NH2 with a disul. de bridge, the Cys-His motif was found to be crucial for the coordination of Ni2+ ions. In the case of the N-unprotected analogues, the N-terminal amino group participates in the coordination as well.
机译:Waglerin I是一种22个氨基酸的蛇毒毒素。由于存在两个Cys和His残基,其三个片段(GGKPDLRPCHP-NH2,PCHYIPRPKPR-NH2,PCHPPCHYIPR-NH2)可能是过渡金属离子的非常有吸引力的配体。这项工作的主要目的是确定这两个相邻残基对Ni2 +离子结合的影响,特别是因为这种基序在自然界中非常普遍,因此对低分子量模型的研究可能有助于理解较大的系统。在这项工作中,使用电位计和光谱法(UV-Vis,CD,EPR和NMR)结合Ni2 +(和Cu2 +用于带有二硫键的肽)对Waglerin片段及其受N保护的类似物进行了研究。在所有肽中,除PCHPPCHYIPR-NH2外均带有二硫键。在桥上,发现Cys-His基序对于Ni2 +离子的配位至关重要。在N-未保护的类似物的情况下,N-末端氨基也参与配位。

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