ABSTRACT
Cholera is one of the earliest infections to be studied by epidemiological methods. Worldwide it affects 3-5 million people and causes 100,000-130,000 deaths a year as of 2010. Cholera is an infection of the small intestine that causes a large amount of watery diarrhea; it is caused by the bacterium vibrio cholerae. The cholera toxin (CTX or CT) is an oligomeric complex made up of six protein subunits a copy of A subunit and the five copies of B subunit, connected by a disulfide bond. This study is based on targeting the CTX using computational tools, a natural metabolite mangiferin was taken and its chemical features are generated using common pharmacophore analysis, using minmaybridge database and taken lead compound were optimized and the Lipinski’s Rule of 5 properties were analyzed. Here, the binding affinity of protein – ligand interaction studied and displayed using ligand fit.
ABSTRACT
Ras proteins play crucial roles in cell growth regulation, signal transduction and proliferation. Abnormal Ras proteins caused by genetic mutations are more common in human cancers. Activation of Ras occurs by enzymatic attachment of Farnesyl moiety by Farnesyl transferase. It has been proven that Ftase is a potential anticancer protein target. In this study we perform a virtual screening using polyphenol derivative from various sources against Ftase and establish ‘Theaflavin’ an antioxidant polyphenol extracted from Camellia sinensis (tea), as a potential inhibitor. This conclusion is further supported by comparative studies of molecular docking and 10 nS molecular dynamics simulation with ‘Tipifarnib’ (Zarnestra) a preclinical Ftase inhibitor.