Int J Pharma Res Health Sci. 2019; 7 (6): 3111-16 3111 IIIIIIIII© International Journal of Pharma Research and Health Sciences. All rights reserved DOI:10.21276/ijprhs.2019.06.08 Kumar Sambhav et al. CODEN (USA)-IJPRUR, e-ISSN: 2348-6465 Original Article In-silico Design of Covalently Bonding Catechol based Urease Inhibitors as Potential Candidates for Treatment of Helicobacter pylori Infection Kumar Sambhav Chopdar 1 , Ganesh Chandra Dash 2 , Pranab Kishor Mohapatra 3 , Binata Nayak 4 , Mukesh Kumar Raval 5, #, * 1 Department of Zoology, Rajendra College, Balangir, Odisha 767002, India. 2 Department of Chemistry, APS College, Roth, Balangir, Odisha 767061, India. 3 Department of Chemistry, CV Raman College of Engineering, Bhubaneswar, Odisha 752054, India. 4 School of Life Sciences, Sambalpur University, Sambalpur, Odisha 768019, India. 5 Department of Chemistry, Gangadhar Meher University, Sambalpur, Odisha 768004, India. ARTICLE INFO ABSTRACT ______ 1. INTRODUCTION Importance of the role of urease in microbial pathogenicity in general and Helicobacter pylori (H. Pylori) induced gastro-duodenal infection in particular is well established [1- 7]. Urease inhibitors may serve as a drug candidate for remedy to urease related pathogenic conditions. In spite of International Journal of Pharma Research and Health Sciences Available online at www.pharmahealthsciences.net Received: 19 Nov 2019 Accepted: 29 Dec 2019 Corresponding author * Mukesh Kumar Raval Department of Chemistry, GangadharMeher University, Sambalpur, Odisha 768004, India. # Present Address: Stone Building, Opposite Mission School, Balangir, Odisha 767001, India E-mail ID: mraval@yahoo.com Design and synthesis of novel urease inhibitors are gaining importance now days with specific context as a remedy to Helicobacter pylori infection. Toxicity and hydrolytic profile of urease inhibitors are deciding factors for success of in vivo and clinical trials. An attempt is made to design covalently bound inhibitors through C-S bond between aromatic ring carbon and sulfur (SG) atom of Cys321 in H. pylori urease, 1e9y. Catechol and p-benzoquinone are known to form such covalent linkage. The catechol ring substituted with an alkyl chain ending with a functional group with potentiality to bind to Ni (II) atoms are designed in silico. These designed inhibitors at one end form covalent linkage at Cys321 at the mouth of the active site while link to Ni (II) deep down the site on the other end. These types of molecules with both ends sticky may serve as highly potent inhibitors of urease hence potent drug candidates against H. pylori infection. The docking scores and acceptable ADMET parameters are also considered in the design. The compounds may serve as novel covalent inhibitors with high specificity, high potency and low toxicity. Key words: Urease inhibitors, covalently bound ligands, Helicobacter pylori, Catechol.