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首页> 外文期刊>International Journal of Peptide Research and Therapeutics >IR, MS and CD Investigations on Several Conformationally-Different Histidine Peptides
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IR, MS and CD Investigations on Several Conformationally-Different Histidine Peptides

机译：几种构型不同的组氨酸肽的IR，MS和CD研究

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摘要

Solid phase synthetic methodology has been used to prepare four peptides which form a system able to monitor metal ion binding to conformationally different peptides. The 19-residues oligopeptides containing histidine residues in various positions of Ala or Gly sequences, namely GGGGHGGGGHGGGGHGGGG, GGGHGGGHGGGHGGGGGGG, AAAAHAAAAHAAAA-HAAAA, and AAAHAAAHAAAHAAAAAAA have been synthesized by Fmoc strategy and characterized by Fourier transform infrared spectroscopy (FT-IR) as well as electrospray ion trap mass spectrometry (ESI-MS) and circular dichroism (CD). The analysis of CD-spectra of the four peptides revealed that the secondary structure depends much on the amino acid sequence. Biological and medical consequences of conformational changes of metal-bound peptides are further discussed.
机译：固相合成方法已用于制备四种肽，它们形成能够监测金属离子与构象不同的肽结合的系统。通过Fmoc策略合成了具有Ala或Gly序列各个位置上的组氨酸残基的19个残基寡肽，即GGGGHGGGGHGGGGHGGGG，GGGHGGGHGGGHGGGGGGGGG，AAAAHAAAAHAAAA-HAAAA和AAAHAAAHAAAHAAAAAAAAAA，并通过傅里叶变换红外光谱（FT-IR）进行了表征。离子阱质谱（ESI-MS）和圆二色性（CD）。四种肽的CD光谱分析表明，二级结构在很大程度上取决于氨基酸序列。金属结合肽的构象变化的生物学和医学后果将进一步讨论。

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