Next Article in Journal
Evolution of the Aroma Volatiles of Pear Fruits Supplemented with Fatty Acid Metabolic Precursors
Next Article in Special Issue
Saikosaponin D Isolated from Bupleurum falcatum Inhibits Selectin-Mediated Cell Adhesion
Previous Article in Journal
Aggregation Behavior of Long-Chain Piperidinium Ionic Liquids in Ethylammonium Nitrate
Previous Article in Special Issue
Anti-Proliferative Effects of Siegesbeckia orientalis Ethanol Extract on Human Endometrial RL-95 Cancer Cells
Article Menu

Export Article

Open AccessArticle
Molecules 2014, 19(12), 20170-20182; doi:10.3390/molecules191220170

Potential Mechanism of Action of meso-Dihydroguaiaretic Acid on Mycobacterium tuberculosis H37Rv

Facultad de Ciencias Químicas, Universidad Autónoma de Nuevo León, Av. Universidad s/n, Ciudad Universitaria, San Nicolás de los Garza, Nuevo León 66451, Mexico
Centro de Biotecnología Genómica, Instituto Politécnico Nacional, Boulevard del Maestro s/n, Col. Narciso Mendoza, Reynosa, Tamaulipas 88710, Mexico
Servicio de Gastroenterología y Departamento de Patología Clínica, Hospital, Universitario Dr. José Eleuterio González, Universidad Autónoma de Nuevo León, Madero y Aguirre Pequeño, Mitras Centro, Monterrey, Nuevo León 64460, Mexico
Author to whom correspondence should be addressed.
Received: 19 September 2014 / Revised: 8 November 2014 / Accepted: 11 November 2014 / Published: 2 December 2014
(This article belongs to the Collection Bioactive Compounds)
View Full-Text   |   Download PDF [1071 KB, uploaded 2 December 2014]   |  


The isolation and characterization of the lignan meso-dihydroguaiaretic acid (MDGA) from Larrea tridentata and its activity against Mycobacterial tuberculosis has been demonstrated, but no information regarding its mechanism of action has been documented. Therefore, in this study we carry out the gene expression from total RNA obtained from M. tuberculosis H37Rv treated with MDGA using microarray technology, which was validated by quantitative real time polymerase chain reaction. Results showed that the alpha subunit of coenzyme A transferase of M. tuberculosis H37Rv is present in both geraniol and 1-and 2-methylnaphthalene degradation pathways, which are targeted by MDGA. This assumption was supported by molecular docking which showed stable interaction between MDGA with the active site of the enzyme. We propose that inhibition of coenzyme A transferase of M. tuberculosis H37Rv results in the accumulation of geraniol and 1-and 2-methylnaphtalene inside bacteria, causing membrane destabilization and death of the pathogen. The natural product MDGA is thus an attractive template to develop new anti-tuberculosis drugs, because its target is different from those of known anti-tubercular agents. View Full-Text
Keywords: Mycobacterium tuberculosis H37Rv; meso-dihydroguaiaretic acid; natural product; mode of action Mycobacterium tuberculosis H37Rv; meso-dihydroguaiaretic acid; natural product; mode of action

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Clemente-Soto, A.F.; Balderas-Rentería, I.; Rivera, G.; Segura-Cabrera, A.; Garza-González, E.; del Rayo Camacho-Corona, M. Potential Mechanism of Action of meso-Dihydroguaiaretic Acid on Mycobacterium tuberculosis H37Rv. Molecules 2014, 19, 20170-20182.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top