L. R. Savalas, Baiq Repika Nurul Furqon, D. Asnawati
Jun 18, 2020
Citations
1
Influential Citations
2
Citations
Quality indicators
Journal
Acta biochimica Polonica
Abstract
Small protein tyrosine phosphatase (PtpA) of Mycobacterium tuberculosis is attributed to the development of latent tuberculosis infection, and hence bocomes an interesting target for drug development. In this communication, inhibition of PtpA by naturally occurring fatty acids cis-2 and trans-2-eicosenoic acid is investigated. Mtb PtpA was heterologously expressed in Escherichia coli, and the activity of PtpA was inhibited by cis-2 and trans-2 eicosenoic fatty acids. Both compunds showed strong inhibition of PtpA activity with IC50 at low micromolar concentration. As comparison, trans-11-eicosenoic acid only slightly inhibit PtpA. In silico analysis confirmed the inhibition of PtpB by cis-2-eicosenoic acid by formation of several hydrogen bonds. These findings show that cis-2 and trans-2 eicosenoic fatty acids are potential candidates for latent tuberculosis inhibitors.