By Arianna Chase and Carrie Garvey
Faculty Mentor: Dr. Davis Oldham
Abstract:
The KasA protein in M. tuberculosis catalyzes the steps of a four-step fatty acid elongation that consequently enables the strength of the TB cell wall. The inhibition of the KasA protein would cause the fatty acid chain to not form and encourage the lysis of M. tuberculosis. The product will be formed through the proposed use of grignard addition, chlorination of alcohol, and SN2 reaction with deprotonated piperidinol product. A HNMR and C13NMR was taken for the final product of all the reactions. The HNMR showed peaks that gave integrals which totaled up to 25 hydrogens and the C13NMR showed a total of 18 peaks, which is short 10 carbons of the final product. However, due to the high number of aromatic carbons expected in the final product, it can be assumed that the aromatic carbons have overlapping peaks and are all present. Three carbons on the C13NMR from 38.67ppm-61.28ppm represent the carbons of the piperidine ring and a peak at 71.48ppm represents the carbon attached to the alcohol. With these results, it was concluded that the desired KasA protein inhibitor product was formed
