Structural stability and aggregation behavior of the VEALYL peptide derived from human insulin: a molecular dynamics simulation study.

Abstract excerpt

The VEALYL peptide from B chain (residues 12-17) of insulin has been shown to form amyloid-like fibrils. Recently, the atomic structure of the VEALYL oligomer has been determined by X-ray microcrystallography and reveals a dry, tightly self-complementing structure between the neighboring beta-sheet layers, termed as "steric zipper." In this study, several molecular dynamics simulations with all-atom explicit...

Topics

Join the communities discussing this publication.

• Amyloid
• Crystallography, X-Ray
• Glycine
• Insulin
• Models, Molecular