纤维
淀粉样纤维
淀粉样蛋白(真菌学)
蛋白质聚集
化学
肽
生物物理学
骨料(复合)
材料科学
体外
纳米结构
纳米技术
生物化学
淀粉样β
生物
疾病
医学
无机化学
病理
作者
Sanjai Kumar Pachahara,C. Subbalakshmi,Ramakrishnan Nagaraj
出处
期刊:Current Protein & Peptide Science
[Bentham Science]
日期:2017-07-06
卷期号:18 (9)
被引量:9
标识
DOI:10.2174/1389203717666160724210122
摘要
Amyloid fibrils, which are implicated in several diseases, are highly ordered structures formed by aggregation of proteins. Intriguingly, several short peptides, some of which are unrelated to the disease-causing proteins, also aggregate to form amyloid fibrils in vitro. The aggregation behavior of these short peptides can be modulated so that they form nanostructures that are not in any way related to amyloid fibrils. These observations have led to extensive research aimed at getting insights into how peptides aggregate to form amyloids as well as non-amyloidogenic structures.This review examines the aggregation behavior of peptides that form highly polymorphic structures including fibrils, nanotubes, nanospheres and hydrogels. The review also describes how short peptides composed of only two and three hydrophobic and aromatic amino acids can selfassemble to form nanotubes and nanospheres.Peptides with widely varying amino acid composition and lengths aggregate to form indistinguishable fibrils and nanostructures. The potential application of these aggregated structures in the design of novel biomaterials is reviewed and highlighted.It is evident that highly polymorphic aggregated structures of peptides can be obtained by varying conditions such as solvent of dissolution, temperatures, pH and even surfaces of deposition.
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