Himani Chaurasia

Bio: Himani Chaurasia is an academic researcher from Allahabad University. The author has contributed to research in topics: Antimicrobial & Docking (molecular). The author has an hindex of 3, co-authored 7 publications receiving 29 citations.

Anti-HIV potential of diarylpyrimidine derivatives as non-nucleoside reverse transcriptase inhibitors: design, synthesis, docking, TOPKAT analysis and molecular dynamics simulations.

Abstract: In view of the low toxicity of NNRTIs in comparison to NRTIs, a new series of diarylpyrimidine derivatives has been designed as NNRTIs against HIV-1. In silico studies using DS 3.0 software have sh...

Wastewater Treatment Through Nanotechnology: Role and Prospects

Abstract: Water is a most crucial and limited resource on the Earth, which has contaminated due to the addition of heavy metals, pathogens, pesticides, and many organic and inorganic substances. Currently, the research has been focused on the sustainable remediation approach for waste reclamation. Therefore, an affordable technology of wastewater treatment could tackle the problem of water. Nanotechnology is an efficient, affordable, effective, and durable method for water treatment. Nanomaterials have several properties such as specific surface area, high reactivity, high degree of functionalization, size-dependent properties, etc., which make them appropriate materials in wastewater treatment. The present chapter comprehensively describes the characteristics of different nanomaterials and their role in the restoration of aquatic ecosystem.

Design, synthesis, and molecular dynamics simulation studies of quinoline derivatives as protease inhibitors against SARS-CoV-2.

Abstract: A new series of quinoline derivatives has been designed and synthesized as probable protease inhibitors (PIs) against severe acute respiratory syndrome coronavirus 2. In silico studies using DS v20.1.0.19295 software have shown that these compounds behaved as PIs while interacting at the allosteric site of target Mpro enzyme (6LU7). The designed compounds have shown promising docking results, which revealed that all compounds formed hydrogen bonds with His41, His164, Glu166, Tyr54, Asp187, and showed π-interaction with His41, the highly conserved amino acids in the target protein. Toxicity Prediction by Komputer Assisted Technology results confirmed that the compounds were found to be less toxic than the reference drug. Further, molecular dynamics simulations were performed on compound 5 and remdesivir with protease enzyme. Analysis of conformational stability, residue flexibility, compactness, hydrogen bonding, solvent accessible surface area (SASA), and binding free energy revealed comparable stability of protease:5 complex to the protease: remdesivir complex. The result of hydrogen bonding showed a large number of intermolecular hydrogen bonds formed between protein residues (Glu166 and Gln189) and ligand 5, indicating strong interaction, which validated the docking result. Further, compactness analysis, SASA and interactions like hydrogen-bonding demonstrated inhibitory properties of compound 5 similar to the existing reference drug. Thus, the designed compound 5 might act as a potential inhibitor against the protease enzyme.Communicated by Ramaswamy H. SarmaHighlightsQuinoline derivatives have been designed as protease inhibitors against SARS-CoV-2.The compounds were docked at the allosteric site of SARS-CoV-2-Mpro enzyme (PDB ID: 6LU7) to study the stability of protein-ligand complex.Docking studies indicated the stable ligand-protein complexes for all designed compounds.The Toxicity Prediction by Komputer Assisted Technology protocol in DS v20.1.0.19295 software was used to evaluate the toxicity of the designed quinoline derivatives.Molecular dynamics studies indicated the formation of stable ligand-Mpro complexes.

Current and Emerging Adsorbent Technologies for Wastewater Treatment: Trends, Limitations, and Environmental Implications

Abstract: Wastewater generation and treatment is an ever-increasing concern in the current century due to increased urbanization and industrialization. To tackle the situation of increasing environmental hazards, numerous wastewater treatment approaches are used—i.e., physical, chemical, and biological (primary to tertiary treatment) methods. Various treatment techniques being used have the risks of producing secondary pollutants. The most promising technique is the use of different materials as adsorbents that have a higher efficacy in treating wastewater, with a minimal production of secondary pollutants. Biosorption is a key process that is highly efficient and cost-effective. This method majorly uses the adsorption process/mechanism for toxicant removal from wastewater. This review elaborates the major agricultural and non-agricultural materials-based sorbents that have been used with their possible mechanisms of pollutant removal. Moreover, this creates a better understanding of how the efficacy of these sorbents can be enhanced by modification or treatments with other substances. This review also explains the re-usability and mechanisms of the used adsorbents and/or their disposal in a safe and environmentally friendly way, along with highlighting the major research gaps and potential future research directions. Additionally, the cost benefit ratio of adsorbents is elucidated.

Binding mechanism and structural insights into the identified protein target of COVID-19 and importin-α with in-vitro effective drug ivermectin.

Abstract: While an FDA approved drug Ivermectin was reported to dramatically reduce the cell line of SARS-CoV-2 by ∼5000 folds within 48 h, the precise mechanism of action and the COVID-19 molecular target involved in interaction with this in-vitro effective drug are unknown yet. Among 12 different COVID-19 targets along with Importin-α studied here, the RNA dependent RNA polymerase (RdRp) with RNA and Helicase NCB site show the strongest affinity to Ivermectin amounting -10.4 kcal/mol and -9.6 kcal/mol, respectively, followed by Importin-α with -9.0 kcal/mol. Molecular dynamics of corresponding protein-drug complexes reveals that the drug bound state of RdRp with RNA has better structural stability than the Helicase NCB site and Importin-α, with MM/PBSA free energy of -187.3 kJ/mol, almost twice that of Helicase (-94.6 kJ/mol) and even lower than that of Importin-α (-156.7 kJ/mol). The selectivity of Ivermectin to RdRp is triggered by a cooperative interaction of RNA-RdRp by ternary complex formation. Identification of the target and its interaction profile with Ivermectin can lead to more powerful drug designs for COVID-19 and experimental exploration.