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The Assembly of Individual Chaplin Peptides from Streptomyces coelicolor into Functional Amyloid Fibrils

机译:卓别林肽链霉菌肽的各个卓别林肽组装成功能性淀粉样蛋白原纤维的过程

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摘要

The self-association of proteins into amyloid fibrils offers an alternative to the natively folded state of many polypeptides. Although commonly associated with disease, amyloid fibrils represent the natural functional state of some proteins, such as the chaplins from the soil-dwelling bacterium Streptomyces coelicolor, which coat the aerial mycelium and spores rendering them hydrophobic. We have undertaken a biophysical characterisation of the five short chaplin peptides ChpD-H to probe the mechanism by which these peptides self-assemble in solution to form fibrils. Each of the five chaplin peptides produced synthetically or isolated from the cell wall is individually surface-active and capable of forming fibrils under a range of solution conditions in vitro. These fibrils contain a highly similar cross-β core structure and a secondary structure that resembles fibrils formed in vivo on the spore and mycelium surface. They can also restore the growth of aerial hyphae to a chaplin mutant strain. We show that cysteine residues are not required for fibril formation in vitro and propose a role for the cysteine residues conserved in four of the five short chaplin peptides.
机译:蛋白质自成淀粉样蛋白原纤维的自缔合为许多多肽的天然折叠状态提供了一种替代方法。虽然淀粉样蛋白原纤维通常与疾病有关,但它们代表某些蛋白质的天然功能状态,例如来自土壤细菌细菌coelicolor的链霉菌蛋白,它们覆盖了气生菌丝体和孢子,使其具有疏水性。我们已经对五种短卓别林肽ChpD-H进行了生物物理表征,以探究这些肽在溶液中自组装形成原纤维的机理。人工合成或从细胞壁分离得到的五种卓别林肽中的每一种均具有表面活性,并且能够在一系列体外溶液条件下形成原纤维。这些原纤维包含高度相似的交叉β核心结构和二级结构,类似于体内在孢子和菌丝体表面形成的原纤维。它们还可以将气生菌丝的生长恢复为卓别林突变株。我们表明,半胱氨酸残基不是体外原纤维形成所必需的,并提出了在五个短卓别林肽中的四个中保守的半胱氨酸残基的作用。

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