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首页> 外文期刊>Biomacromolecules >Synthesis and Mass Spectrometric Characterization of a Metal-Affinity Decapeptide: Copper-Induced Conformational Changes
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Synthesis and Mass Spectrometric Characterization of a Metal-Affinity Decapeptide: Copper-Induced Conformational Changes

机译：金属亲和性十肽的合成和质谱表征：铜诱导的构象变化

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摘要

A decapeptide with high affinity toward heavy metal ions (RCHQYHHNRE) has been prepared by Fmoc strategy using TGR resin as solid support. The model peptide provides a simple system that can be used for a systematic study of the impact of different metal ions on peptide secondary structure on a molecular level; histidine residues were incorporated into the peptide in a sequence similar to beta-amyloid peptide (Abeta 1-40) to generate possible complexation sites for Cu~(2+) ions. The peptide secondary structure, as investigated by circular dichroism, and self-assembled nanostructures were observed to depend strongly on the presence of copper and sodium dodecyl sulfate (SDS). Atomic force microscopy (AFM) revealed also that copper and SDS affected slightly the Abeta 1-40) nanostructures. An explanation for the effect of metal ions and SDS on the self-assembly of peptides was proposed. The extensive beta-sheet formation may further promote peptide self-assembly into longer fibers.
机译：使用TGR树脂作为固体载体，通过Fmoc策略制备了对重金属离子具有高亲和力的十肽（RCHQYHHNRE）。模型肽提供了一个简单的系统，可用于在分子水平上系统研究不同金属离子对肽二级结构的影响;组氨酸残基以类似于β-淀粉样肽（Abeta 1-40）的顺序掺入肽中，以生成Cu〜（2+）离子可能的络合位点。通过圆二色性研究的肽二级结构和自组装的纳米结构在很大程度上取决于铜和十二烷基硫酸钠（SDS）的存在。原子力显微镜（AFM）还显示，铜和SDS对Abeta 1-40）纳米结构有轻微影响。提出了金属离子和SDS对肽自组装的影响的解释。大量的β-折叠形成可进一步促进肽自组装成更长的纤维。

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