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Tuberculosis (TB) is returning as an important public health problem in light of the AIDS epidemic and advent of multidrug (MDR TB) and extensive resistant (XDR TB) tuberculosis strains. The enzymes involved in the mycobacterial cell wall biosynthesis represent excellent drug targets, as many of them are not present in mammalian cells. UDP-galacto pyranose mutase (UDP-Galp mutase) is one of the two key enzymes involved in the biosynthesis of galactan, a fundamental component of the mycobacterial cell wall. This book provides chemists and tuberculosis professionals with methods by which 4-substituted thiazole ester can be prepared by a cyclisation of an -L-cysteine ester and aldehyde in the synthesis UDP-Galp mutase inhibitor N-{2-[1-(2- 1H-indo-3-yl-acetyl)-piperidine-4-yl]-thiazole-4- carbonyl}hydrazine carboxylate discovered by in silico virtual screening of theTripos LeadQuest© library using the FlexX docking program in sufficient yield for the inhibition kinetics study and cocrystallization with the target enzyme. The drug inhibitory effects will act as a hit´ to form the basis of new leads allowing new medication to be developed to control tuberculosis.

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Olajide A. Mustapha, B.Sc., M.Sc., MRes., MRSC., C.Chem. Studied Chemistry at University of Ilorin and Masters of Research in Chemistry at University of Nottingham, UK. Principal Lecturer at Federal Polytechnic Offa, Nigeria. Currently Postgraduate Researcher (Analytical/Forensic Chemistry) at Nottingham Trent University, UK.

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