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Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry (CCMS)
Published on: December 20, 2010
Targeting SAM-dependent methyltransferase in Mycobacterium avium complex (MAC) with natural products: ADMET and
Anindita Banerjee1, Saubashya Sur1
1Postgraduate Department of Botany, Life Sciences Block, Ramananda College, Bishnupur, West Bengal 722122 India.
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The Mycobacterium avium complex (MAC) comprises non-tuberculous mycobacteria that cause respiratory infections in vulnerable humans and diseases in animals. Treating these infections is problematic owing to the persistence of MAC inside hosts, antibiotic resistance, and adverse side effects. SAM-dependent methyltransferase is a key enzyme altering lipids and metabolites, as well as regulates cell wall permeability and virulence. Specifically, the ability of SAM-dependent methyltransferase to modify mycolic acid has made it a drug target for fighting persistent infections. To prevent the increasing MAC infections, targeting virulent genes and the discovery of novel drugs are necessary. Moreover, because of the limitations of existing therapies, alternative strategies are essential. This in silico analysis emphasised screening natural products, assessing their pharmacokinetic and toxicity properties, molecular docking with the SAM-dependent methyltransferase of MAC, followed by molecular simulations. The intention was to detect lead compounds acting against SAM-dependent methyltransferase. In this regard, eight natural products with suitable ADMET properties were finalised. Artificial intelligence-based modelling of SAM-dependent methyltransferase generated high-quality three-dimensional structures. Their molecular docking with the eight natural products identified docked complexes with binding energies ranging from - 4.7 to -10.3 kcal/mol. Molecular simulations with iMODS confirmed the stability and robustness of the docking complexes. Notably, demethoxycurcumin (-10.3 kcal/mol) and bisdemethoxycurcumin (-10.2 kcal/mol) exhibited superior binding affinities with the SAM-dependent methyltransferase of M. avium 104. These were the top compounds targeting SAM-dependent methyltransferase. This research provided evidence for drug target identification, although further experimental validation is required to translate this in silico outcome into clinical use.
Supplementary Information:
The online version contains supplementary material available at 10.1007/s40203-026-00710-8.
