Backbone N-Amination Promotes the Folding of β-Hairpin Peptides via a Network of Hydrogen Bonds.

ABSTRACT: Molecular dynamics (MD) simulations have been used to characterize the effects of backbone N-amination of residues in a model β-hairpin peptide. This modification is of considerable interest as N-aminated peptides have been shown to inhibit amyloid-type aggregation. Six derivatives of the β-hairpin peptide, which contain one, two, or four N-aminated residues, have been studied. For each peptide 100 ns MD simulations starting from the folded β-hairpin structure were performed. The effects of the N-amination prove to be very sequence dependent. N-Amination of a residue involved in interstrand hydrogen bonding (Val3) leads to unfolding of the β-hairpin, whereas N-amination of a residue toward the C-terminus (Leu11) gives fraying at the termini of the peptide. In the other derivatives the pept

SUBMITTER: Dolenc J 

PROVIDER: S-EPMC9795546 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature