来自含非编码氨基酸的三肽的淀粉样纤维形成β-折叠聚集体的首个晶体学特征。
First crystallographic signature of amyloid-like fibril forming beta-sheet assemblage from a tripeptide with non-coded amino acids.
作者信息
Maji S K, Drew M G, Banerjee A
机构信息
Department of Biological Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Calcutta-700 032, India.
出版信息
Chem Commun (Camb). 2001 Oct 7(19):1946-7. doi: 10.1039/b105418j.
The model tripeptide Boc-beta-Ala(1)-Aib(2)-beta-Ala(3)-OMe 1 [beta-Ala: beta-alanine, Aib: alpha-aminoisobutyric acid] forms an infinite parallel beta-sheet structure through intermolecular interactions in single crystals and from the SEM diagram of this peptide, it is evident that the compound has fibrillar morphology, a characteristic of neurodegenerative disease causing amyloid aggregate.
模型三肽Boc-β-丙氨酸(1)-α-氨基异丁酸(2)-β-丙氨酸(3)-甲酯1[β-丙氨酸：β-丙氨酸，α-氨基异丁酸：α-氨基异丁酸]在单晶中通过分子间相互作用形成无限平行β-折叠结构，并且从该肽的扫描电子显微镜图可以明显看出，该化合物具有纤维状形态，这是导致淀粉样聚集的神经退行性疾病的一个特征。
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