https://scholars.lib.ntu.edu.tw/handle/123456789/406729
標題: | Examining the inhibitory actions of copolypeptides against amyloid fibrillogenesis of bovine insulin | 作者: | Kao C.-Y. Lai J.-K. Lin T.-H. Lin Y.-J. Jan J.-S. Wang S.S.-S. |
關鍵字: | Aggregation;Amyloid diseases;Amyloid fibril;Biophysical chemistry;Inhibition;Insulin;Polypeptides;Protein | 公開日期: | 2013 | 卷: | 78 | 起(迄)頁: | 181-188 | 來源出版物: | Biochemical Engineering Journal | 摘要: | Amyloid fibrillogenesis has been involved in at least 40 different degenerative diseases. The 51-residue polypeptide hormone insulin, which is associated with type II diabetes, has been demonstrated to fibrillate in vitro. With bovine insulin as a model, the research presented here examines the influence of two simple, unstructured d,l-lysine-co-glycine (d,l-lys-co-gly) and d,l-lysine-co-L-phenylalanine (d,l-lys-co-phe) copolypeptides, on the in vitro fibril formation process of bovine insulin at pH 2.0 and 55. ¢XC. Our results showed that amyloid fibrillogenesis of insulin may be suppressed by both copolypeptides in a concentration-dependent fashion. In addition, the copolypeptides with higher molar fractions of glycine or l-phenylalanine residue, which are considered to possess higher hydrophobic interacting capacities, demonstrated the superior inhibitory potency against insulin fibril formation. Our findings suggest that the association of insulin and copolypeptides, which is likely dominated by hydrophobic interactions and hydrogen bonding, may mitigate the extent of insulin fibrillogenesis. We believe the results from this work may contribute to the understanding of the molecular factors affecting amyloid fibrillation and the molecular mechanism(s) of the interactions between the unstructured polypeptides and amyloid-forming proteins. ? 2013 Elsevier B.V. |
URI: | https://scholars.lib.ntu.edu.tw/handle/123456789/406729 | ISSN: | 1369703X | DOI: | 10.1016/j.bej.2013.03.023 | SDG/關鍵字: | Amyloid disease; Amyloid fibril; Biophysical chemistries; Concentration-dependent; Degenerative disease; Hydrophobic interactions; Molecular mechanism; Polypeptide hormones; Agglomeration; Amino acids; Enzyme inhibition; Glycoproteins; Hydrogen bonds; Hydrophobicity; Mammals; Polypeptides; Proteins; Insulin; amyloid; bovine insulin; glycine; phenylalanine; polypeptide; article; controlled study; hydrogen bond; hydrophobicity; pH; priority journal; Bovinae |
顯示於: | 化學工程學系 |
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