Examining the inhibitory actions of copolypeptides against amyloid fibrillogenesis of bovine insulin
Journal
Biochemical Engineering Journal
Journal Volume
78
Pages
181-188
Date Issued
2013
Author(s)
Abstract
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.
Subjects
Aggregation
Amyloid diseases
Amyloid fibril
Biophysical chemistry
Inhibition
Insulin
Polypeptides
Protein
SDGs
Other Subjects
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
Type
journal article