Journal article Open Access
Abinash Pandit*1, S.N. Sriharsha1, N. Habeela Jainab1, Praveen P2, Sheshagiri R Dixit2
N-Substituted sulfonamide anthranilate hydroxamic acid derivatives have a better binding affinity towards the Matrix Metalloprotease (MMP) enzyme as per the literature. Based on that we have selected the Matrix Metalloprotease-1 (MMP-1) domain of MMP enzyme and performed the molecular docking studies using the SYBYL X 2.1 software. We have designed fifteen new chemical new entities for the docking studies and among that two chemical entities were found to have better binding affinities towards the MMP-1 target. By studying the total docking scores of all the new chemical entities we have concluded that the groups like benzyl group at Nth position, methoxy group at 4th position of phenyl sulfonamide nucleus, dimethylamine group at 3rd position of hydroxyl benzamide nucleus, etc. are responsible for better activities and binding affinities towards MMP-1 target. So, based on that we can proceed for the further synthesis of those molecules which has higher affinities towards the MMP domains. Some of the positions like 4th, 6th position in Hydroxy Benzamide Nucleus and 2nd, 3rd, 5th, 6th positions in Phenyl Sulfamido Nucleus are unsubstituted and still, we are in process of study in the future projects.