ABSTRACT
Matrix metalloproteinases (MMPs) are secreted in the body from various proinflammatory cells and connective tissues, namely osteoblasts, fibroblasts, endothelial cells, neutrophils, lymphocytes, and macrophages. It is important to have a thorough knowledge regarding the prime amino acid residues at the respective active sites of MMPs and their binding patterns of interactions and orientations with respective MMPIs to improve activity and selectivity. While binding, both MMPI and the active site amino acids need stability. Amino acids forming various hydrophobic pockets offer various dynamic characteristics due to the variations of amino acids present in the Ω-loop and S1′ pocket. Regarding MMPIs, most of these MMPIs are designed to comprise a ZBG group that coordinates to the catalytic Zn2+ ion with good affinity. Similarly, the dynamic behavior of other hydrophobic pockets should also be taken into consideration.
