ArticleIn silico pharmacology2025
Computational studies of natural product compound (CP-225917) for lead identification.
Article in In silico pharmacology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
In this investigation, a computational analysis of CP-225,917 (a natural product compound isolated from unidentified fungi) on the farnesyl transferase (FTase) enzyme has been performed using docking, PLIF, and molecular dynamics (MD) simulations methodologies to understand its binding interactions. The crystallographic structure of the FTase used for the study was obtained from the Protein Data Bank (PDB id 3E37), and docking, MD simulations, MMPBSA, and PLIF analysis were performed with Autodock 4.2, AMBER 12, and MOE software, respectively. The results showed that the residues such as Lys164, Tyr166, His201, ArgB202, HisB248, TyrB300, LysB356, TyrB361, HisB362, and ZnC1001 have predominantly contributed to the interactions with the molecules through side chain (hydrogen bond acceptor and donor), backbone (hydrogen bond acceptor and donor), surface, and ionic interactions. The aromatic rings in TyrB300 and TyrB361 form surface interactions, and the side chains of all these residues show hydrogen bonding interactions with the molecule. The ionic interaction also formed between the molecules and the residues (LysB356 and Zn Supplementary Information: The online version contains supplementary material available at 10.1007/s40203-025-00405-6.
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