Inhibiting, promoting, and preserving stability of functional protein fibrils

Inhibiting, promoting, and preserving stability of functional protein fibrils
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DOI:
10.1039/c1sm06643a
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发表时间:
2012-01-01
期刊:
影响因子:
3.4
通讯作者:
Mezzenga, Raffaele
Mezzenga, Raffaele
中科院分区:
化学2区
文献类型:
--
作者:
Jones, Owen Griffith;Mezzenga, Raffaele

文献摘要

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蛋白原纤维不仅与医学和淀粉样蛋白相关的神经退行性疾病有关,而且在材料科学或生物学中也具有功能结构。根据所选择的环境条件和与合适组分的相互作用,可以促进或抑制蛋白质组装成原纤维。我们在此回顾在生理和非生理条件下促进和抑制蛋白纤颤的关键策略,以创建功能设计。讨论的主要变量是溶剂条件、金属/离子、生物聚合物、芳香族化合物和表面活性成分。由于研究方向的偏倚,传统上对纤维性颤动的抑制进行了更深入的研究,但最近重点转移了。因此,尽管提出了各种策略来分解成熟蛋白原纤维,但重点是给出了导致所产生的原纤维刚性和长度增加的方法。我们强调了这一领域中需要进一步发展的重要领域和未来实验的有希望的方向。
Protein fibrils are relevant not only in medicine and amyloid-related neurodegenerative diseases, but also as functional structures in material science or biology. The assembly of protein into fibrils can be promoted or inhibited based on the chosen environmental conditions and interaction with suitable components. We review here the key strategies for promotion and inhibition of protein fibrillation in both physiological and non-physiological conditions in order to create functional designs. The major variables discussed are solvent conditions, metals/ions, biopolymers, aromatic compounds, and surface active components. Due to bias in research directions, deeper investigation has traditionally been carried out for inhibition of fibrillation, but focus has recently shifted. Thus, while various strategies are presented on the breakdown of mature protein fibrils, emphasis is given to the approaches leading to increased rigidity and length of resultant fibrils. We highlight important areas in this field that require further development and promising lines of future experiments.