Molecular dynamics study of early events during photooxidation of eye lens protein γB-crystallin

Abstract

Molecular dynamics modeling on 200 ps time scale was used to study bovine eye lens protein γB-crystallin (GCS) and two possible products of its photooxidation. The mutations were done at positions of tryptophan (Trp) residues which were changed into N-formylkynurenine (NFK) in position 42 (1NFK) or in positions 42, 68, 131 and 157 (4NFK). Quantum chemical calculations using the DFT, HF and AM1 methods were performed for both Trp and NFK. The stronger hydrophilic character of NFK results in structural rearrangements in the regions related to disulfide bridges formation. The protein mutations studied may have impact on the cataract formation.