Probing the Nature of Noncovalent Interactions in Dimers of Linear Tyrosine-Based Dipeptides.

ABSTRACT: Tyrosine-based dipeptides self-assemble to form higher order structures. To gain insights into the nature of intermolecular interactions contributing to the early stages of the self-assembly of aromatic dipeptides, we study the dimers of linear dityrosine (YY) and tryptophan-tyrosine (WY) using quantum-chemical methods with dispersion corrections and universal solvation model based on density in combination with energy decomposition and natural bond orbital (NBO) analyses. We find that hydrogen bonding is a dominant stabilizing force. The lowest energy structure for the linear YY dimer is characterized by O_carboxyl···H(O)_tyr. In contrast, the lowest energy dimer of linear WY is stabilized by O_carboxyl···H(N)_trp and π_tyr···π_tyr

SUBMITTER: Mayes ML 

PROVIDER: S-EPMC6648619 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature