MOLECULAR DOCKING STUDIES TOWARDS DEVELOPMENT OF NOVEL GLY-PHE ANALOGS FOR POTENTIAL INHIBITION OF CATHEPSIN C (DIPEPTIDYL PEPTIDASE I)
Umesh Kalathiya, Monikaben Padariya, Michał Jewgiński, Maciej Bagiński · International Journal for Computational Biology · 2014
Cathepsin C is a cysteine protease required for activation of various pro-inflammatory serine proteases and, essentially, is of interest as a therapeutic target. Cathepsin C coordinate system was employed as a model to study the interaction of some already available inhibitors of Cathepsin C. Compounds containing Gly-Phe fragment with functional groups at its ends were designed by knowledge based approach. Using AutoDock and Discovery Studio Client 3.1 software packages, binding energy of different conformations and ten scoring functions (LigScore1, LigScore2, PLP1, PLP2, JAIN, PMF, PMF04, LUDI_1, LUDI_2 and LUDI_3) were calculated for newly designed compounds. These docking studies revealed favorable energy scores which also helps to understand interaction of ligands with enzyme.