Comprehensive Computational Investigation of 𝑹𝒚𝒏𝒄𝒉𝒐𝒕𝒆𝒄𝒉𝒖𝒎 𝒆𝒍𝒍𝒊𝒑𝒕𝒊𝒄𝒖𝒎 for Neuro-Pharmacological Activity: Molecular Docking, Molecular Dynamics and Pre-ADMET Analysis
نویسندگان
1 Faculty of Pharmaceutical Science, Assam down town University, Sankar Madhab Path, Gandhi Nagar, Panikhaiti, Guwahati, Assam, India
2 Faculty of Pharmaceutical Sciences, Rama University, Rama City, Mandhana, Kanpur, Uttar Pradesh 209 217, India
3 Department of Chemistry and Biochemistry, Lamar University, 4400 S M L King Jr Pkwy, Beaumont, TX 77705, USA
4 Joginpally B.R. Pharmacy College, Yenkapally, Moinabad, Hyderabad, Telangana 500075, India.
5 Department of Pharmaceutics, Pannai College of pharmacy, Dindigul, Tamil Nadu, India
6 School of Pharmacy, Anurag university, Hyderabad, Telangana 500088, India
7 Department of Pharmacology, Centurion University of Technology and Management, Bhubaneswar, odisha-752050, India
8 Department of Pharmaceutics, School of Pharmacy, Anurag University, Hyderabad, Telangana 500088, India
9 Department of Pharmaceutical Analysis and Quality Assurance, Royal College of Pharmacy and Health Sciences, Berhampur, Odisha 760002, India
10 Department of Pharmacy Practice, JKKMMRF College of Pharmacy, Komarapalayam, Namakkal, Tiruchengode, Tamil Nadu 638183, India
doi
10.48309/ajca.2025.530834.1869چکیده
Rynchotechum ellipticum has shown promising neuropharmacological potential, particularly owing to its antioxidant and neuroprotective properties. Preliminary studies have suggested that its bioactive compounds may modulate neurotransmitter systems and help mitigate neurodegenerative processes, making it a candidate for further neurological research. To pinpoint the phytocompounds responsible for the neuropharmacological activity, a detailed docking study was performed on the phytocompounds of R. ellipticum using GABA protein as the molecular target. Among the studied compounds, stigmasterol exhibited the highest docking score (6.727 kcal/mol), suggesting a strong binding affinity for the GABA receptor. Notably, the terminal phenolic group of stigmasterol formed a hydrogen bond with Asp192. This interaction is significant, as hydrogen bonds often contribute to the specificity and strength of ligand-receptor interactions. In addition to hydrogen bonding with Asp192, stigmasterol also engages in van der Waals interactions with various residues surrounding its binding site. These residues include Arg194, Ser195, Trp196, Asn60, Tyr58, Val203, Gln204, Ser205, Ser206, Thr207, Tyr210, Val212, Ala161, Tyr160, Ser159, Gly158, Lys156, and Pro140. The presence of multiple van der Waals interactions suggests a stable binding conformation, which may enhance the pharmacological effects of stigmasterol. Complex network of hydrogen bonds, hydrophobic interactions, ionic interactions, and water-mediated bonds works synergistically to stabilize stigmasterol within the GABA receptor, ensuring a promising binding that is essential for the receptor’s sedative effect. From present analysis, we conclude that stigmasterol may be responsible for the pharmacological activity of R. ellipticum. We aimed to report the isolation and in vitro enzyme assays of stigmasterol using selected enzymes.
