De novo design and spectroscopic characterization of a dinucleating copper-binding pentadecapeptide.
De novo design and spectroscopic characterization of a dinucleating copper-binding pentadecapeptide.
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双核铜结合十五肽的从头设计和光谱表征。
DOI：
10.1021/ic051577q
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发表时间：
2006
期刊：
影响因子：
--
通讯作者：
DeRose,VictoriaJ
中科院分区：
文献类型：
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作者：
Rockcliffe,DavidA;Cammers,Arthur;Murali,Ayaluru;Russell,WilliamK;DeRose,VictoriaJ
对Ac− WGHGHGPGHGHGH − NH 2（HGP）水溶液的光谱研究表明，铜（II）与肽结合，在铜配位环境中与四个氮原子形成2：1的Cu 2 +/HGP络合物。电子顺磁共振（EPR）和紫外可见光数据表明铜通过肽骨架和咪唑氮供体结合。圆二色性数据显示，HGP在pH 5.5以下是未结合的，并且在pH 9及以上是铜饱和的。脱辅基肽的形式在溶液中是非结构化的，在碱性pH下，在2 mol equiv的Cu 2+存在下，脱辅基肽被组织成一个转角构象。在g = 2区域和pH 7−11范围内，对2：1 Cu 2 +/HGP溶液的EPR测量显示出轴向光谱。Cu 2 +/HGP复合物的分子力学最小化模型给出了8 Å的Cu···Cu分离。
A spectroscopic study of aqueous solutions of Ac−WGHGHGHGPGHGHGH−NH2(HGP) indicates that copper(II) binds to the peptide to form a 2:1 Cu2+/HGP complex with four nitrogen atoms in the copper coordination environment. Electron paramagnetic resonance (EPR) and UV−visible data suggest copper binding through the peptide backbone and imidazole nitrogen donors. Circular dichroism data show that HGP is unbound below pH 5.5 and is copper-saturated at pH 9 and above. The apo form of the peptide is unstructured in solution and is organized into a turn conformation in the presence of 2 mol equiv of Cu2+at basic pH. EPR measurements for 2:1 Cu2+/HGP solutions in theg= 2 region and within the pH range 7−11 exhibit axial spectra. A molecular-mechanics-minimized model of the Cu2+/HGP complex gave a Cu···Cu separation of 8 Å.