Molecular mechanics and dynamics studies on the interaction of gallic acidwith collagen-like peptides

Molecular modelling approaches have been used to understand the interaction of collagen-like peptides with gallic acid, which mimic vegetable tanning processes involved in protein stabilization. Several interaction sites have been identified and the binding energies of the complexes have been calcul ated. The calculated binding energies for various geometries are in the ran ge 6-13 kcal/mol. It is found that some complexes exhibit hydrogen bonding, and electrostatic interaction plays a dominant role in the stabilization o f the peptide by gallic acid. The pi -OH type of interaction is also observ ed in the peptide stabilization. Molecular dynamics (MD) simulation for 600 ps revealed the possibility of hydrogen bonding between the collagen-like peptide and gallic acid. (C) 2001 Elsevier Science B.V. All rights reserved .