具有βXaaHisGlyHis 序列的肽的不寻常协调能力。肽链结构修饰对铜（II）结合的影响。
The unusual coordination abilities of the peptides with betaXaaHisGlyHis sequence. The influence of structural modification of the peptide chain on the copper(II) binding.
机构信息
Department of Inorganic Chemistry, Wrocław Medical University, Szewska 38, 50-139, Wrocław, Poland.
出版信息
Dalton Trans. 2010 Jul 28;39(28):6518-23. doi: 10.1039/b923371g. Epub 2010 Jun 11.
The coordination abilities of tetrapeptides containing beta-amino acids towards Cu(II) ions are presented. The studied tetrapeptides were: Ac-betaAlaHisGlyHis, betaAlaHisGlyHis, Ac-betaAspHisGlyHis, betaAspHisGlyHis, Ac-betaAspHisGly-dHis and betaAspHisGly-dHis. Thorough potentiometric titrations were carried out to establish the stoichiometry of the resulting metal-ligand complexes and the role of free -alphaCOO(-) side chain group in metal binding. The copper(II) coordination mode of the complexes was investigated by performing detailed spectroscopic analyses (UV-Vis, EPR, CD) in strict correlation with potentiometric measurements.
呈现了含有β-氨基酸的四肽与 Cu(II) 离子的配位能力。研究的四肽为：Ac-βAlaHisGlyHis、βAlaHisGlyHis、Ac-βAspHisGlyHis、βAspHisGlyHis、Ac-βAspHisGly-dHis 和 βAspHisGly-dHis。通过详细的电位滴定实验确定了生成的金属-配体配合物的化学计量比，并研究了游离 -αCOO（-）侧链基团在金属结合中的作用。通过与电位测量严格相关的详细光谱分析（UV-Vis、EPR、CD）研究了配合物的铜（II）配位模式。
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