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首页> 外文期刊>Biochimica et biophysica acta: BBA: International journal of biochemistry, biophysics and molecular biololgy. Proteins and Proteomics >Scaffolded multimers of hIAPP(20-29) Peptide fragments fibrillate faster and lead to different fibrils compared to the free hIAPP(20-29) peptide fragment
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Scaffolded multimers of hIAPP(20-29) Peptide fragments fibrillate faster and lead to different fibrils compared to the free hIAPP(20-29) peptide fragment

机译：与游离的hIAPP（20-29）肽片段相比，hIAPP（20-29）肽片段的支架多聚体的原纤化更快，并导致不同的原纤维

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摘要

Applying fibril-forming peptides in nanomaterial design is still challenged by the difficulties in understanding and controlling how fibrils form. The present work investigates the influence of motional restriction on peptide fibrillation. We use cydotriphosphazene and cyclodextrin as templates to make conjugates of the fibril-forming core of human islet amyloid polypeptide. Attachment of the peptide to the templates resulted in multimers containing six peptide fragments at different positions. ThT fluorescence, CD and FTIR spectroscopy, and AFM and TEM imaging reveal that in both conjugates the peptide retained its fibrillating properties and formed fibrils. However, the conjugate fibrils formed more rapidly than the free peptide and were long and thin, as opposed to the thick and twisted morphology of the intact peptide. Thus the motional restrictions introduced by the scaffold modulate the structure of the fibrils but do not impede the actual fibrillation process. (C) 2015 Elsevier B.V. All rights reserved.
机译：在理解和控制原纤维的形成方面的困难仍然使在纳米材料设计中应用原纤维形成的肽面临挑战。本工作研究了运动限制对肽原纤化的影响。我们使用环三磷腈和环糊精作为模板来制作人胰岛淀粉样多肽原纤维形成核心的共轭物。肽与模板的连接导致多聚体在不同位置含有六个肽片段。 ThT荧光，CD和FTIR光谱以及AFM和TEM成像表明，在两种缀合物中，该肽均保留了其原纤化特性并形成了原纤。然而，与完整肽的厚而扭曲的形态相反，缀合物原纤维的形成比游离肽更快并且长而细。因此，由支架引入的运动限制调节了原纤维的结构，但并不妨碍实际的原纤化过程。 （C）2015 Elsevier B.V.保留所有权利。

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