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Structural basis for the formation of soy protein nanofibrils

机译:形成大豆蛋白纳米纤维的结构基础

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摘要

Amyloid-like protein nanofibrils (PNFs) can assemble from a range of different proteins including disease-associated proteins, functional amyloid proteins and several proteins for which the PNFs are neither related to disease nor function. We here examined the core building blocks of PNFs formed by soy proteins. Fibril formation at pH 2 and 90 degrees C is coupled to peptide hydrolysis which allows isolation of the PNF-forming peptides and identification of them by mass spectrometry. We found five peptides that constitute the main building blocks in soy PNFs, three of them from the protein b-conglycinin and two from the protein glycinin. The abilities of these peptides to form PNFs were addressed by amyloid prediction software and by PNF formation of the corresponding synthetic peptides. Analysis of the structural context in the native soy proteins revealed two structural motifs for the PNF-forming peptides: (i) so-called b-arches and (ii) helical segments involved in quaternary structure contacts. However, the results suggest that neither the native structural motifs nor the protein of origin defines the morphology of the PNFs formed from soy protein isolate.
机译:淀粉样蛋白样蛋白纳米纤维(PNFS)可以由一系列不同的蛋白质组装,包括疾病相关蛋白质,官能淀粉样蛋白和几种蛋白质,其中PNF既不与疾病也不有效。我们在这里检查了大豆蛋白形成的PNF的核心积木。在pH 2和90℃下的原纤维形成与肽水解偶联,允许通过质谱分离形成PNF形成肽和鉴定它们。我们发现五种肽,其构成大豆PNF中的主结构块,其中三个来自蛋白质B-甘氨酸的蛋白质B-甘氨酸和两种。通过淀粉样蛋白预测软件和相应的合成肽的PNF形成来解决这些肽形成PNF的能力。对天然大豆蛋白中的结构背景的分析显示了用于PNF形成肽的两个结构基序:(i)所谓的B拱和(II)螺旋段,参与第四节结构接触。然而,结果表明,天然结构基序和原产蛋白质既不确定由大豆蛋白分离物形成的PNF的形态。

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  • 来源
    《RSC Advances》 |2019年第11期|共10页
  • 作者单位

    KTH Royal Inst Technol Dept Chem Stockholm Sweden;

    KTH Royal Inst Technol Dept Chem Stockholm Sweden;

    KTH Royal Inst Technol Dept Chem Stockholm Sweden;

    KTH Royal Inst Technol Dept Chem Stockholm Sweden;

    KTH Royal Inst Technol Dept Chem Stockholm Sweden;

    KTH Royal Inst Technol Dept Chem Stockholm Sweden;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 化学;
  • 关键词

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