Weak intra and intermolecular interactions via aliphatic hydrogen bonding in piperidinium based ionic Liquids: Experimental, topological and molecular dynamics studies

Panja, Sumit Kumar; Kumar, Sumit

doi:10.1016/j.molliq.2023.121354

Cited by 9 publications

(1 citation statement)

References 55 publications

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“…Hydrogen bonding 129 distances are 2.17, 2.19, 3.19, 2.50Å with Tyr279, Pro289, Ile291, respectively. These hydrogen bonding are also responsible for the stability of various molecular system [22][23][24][25][26]. Gly275a, Glu270a, Leu271a, Phe219a, Trp218a.…”

Section: Oxa1 Against Sars-cov-2mentioning

confidence: 99%

Study of Oxadiazole derivatives as precursor for multi-functional inhibitor to SARS-CoV-2: A detailed virtual screening analysis

Kumar,

Kumar

2024

Mong. J. Chem.

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SARS-CoV-2, the virus responsible for the COVID-19 pandemic, is highly contagious and has caused widespread loss of life. In the quest to find effective antiviral agents, attention has turned to oxadiazole derivatives, which are known for their potential antiviral properties in such as CoViTris2020, ChloViD2020, etc. To evaluate their effectiveness, molecular docking and molecular dynamics simulations are conducted for various oxadiazole derivative in interactions with critical proteins involved in the viral infection process. These proteins encompass transmembrane-serine-2 (TMPRSS2), 3-chymotrypsin-like-protease (3CLpro), angiotensin-converting-enzyme-2 (ACE2), and papain-like-protease (PLpro). The study shows that the oxadiazole derivatives exhibited their most stable complexes when interacting with TMPRSS2 in comparison to 3CLpro, ACE2, and PLpro. In particular, Oxa8 displayed a binding energy of -6.52 kcal/mol with TMPRSS2. In contrast, the binding energies with ACE2, 3CLpro, and PLpro were -5.74, -4.56, and -5.56 kcal/mol, respectively. RMSD analysis during MD simulations demonstrated that the complex structure remained consistently stable. During the initial 2 ns, the RMSD value for the ligand concerning its interaction with the protein backbone hovered around 2 Å, indicating a sustained level of structural stability. In conclusion, this study suggests that oxadiazole derivative Oxa8 holds promise as a potential inhibitor of SARS-CoV-2, particularly due to its strong binding affinity with TMPRSS2 and its enduring structural stability observed in molecular dynamics simulations.

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