Biology subjects

Zinnah, K. M. A.

Publications and source records attributed to Zinnah, K. M. A..

3 recordsLinked to original sources

bioRxiv2026

Multi-Target In Silico Investigation of Withaferin A as a Potential Antiviral Inhibitor Against Key Marburg Virus Proteins

Marburg virus (MARV) is a highly pathogenic filovirus that causes hemorrhagic fever with a high mortality rate, with very limited treatment options. The urgent need for targeted antiviral agents emphasizes the importance of structure-based drug discovery approaches. The present study aimed to evaluate the antiviral potential of Withaferin A (PubChem CID-265237) against three key proteins of MARV: viral protein 35 (VP35), and nucleoproteins (NP). Three-dimensional structures of these proteins were retrieved from RCSB-Protein Data Bank and docked with Withaferin A using AutoDock Vina. The ligand demonstrated favourable binding affinities towards all three viral targets, indicating strong interaction potential at functionally relevant sites. Drug-likeness and pharmacokinetic properties predicted using SwissADME and pkCSM indicated acceptable ADMET profiles that comply with key drug-like criteria. To validate the stability of the docking, molecular dynamics simulations (GROMACS, 100 nanoseconds) were conducted. The protein-ligand complexes exhibited stable root mean square deviation (RMSD), root mean square fluctuation (RMSF), and consistent hydrogen bonding patterns throughout the simulation. The MM-GBSA binding free energy analysis further supported favorable binding energetics, predominantly driven by van der Waals and electrostatic interactions. Altogether, these findings demonstrate that Withaferin A exhibits promising multi-target inhibitory potential against key MARV proteins. This study provides molecular insights into ligand-protein interactions and supports further experimental validation of Withaferin A as a potential therapeutic candidate against Marburg virus.

bioinformatics↗

bioRxiv2024

Exploring Harmala Alkaloids as Novel Antimalarial Agents against Plasmodium falciparum through Bioinformatics Approaches

Malaria, caused by the Plasmodium falciparum, remains a significant global health challenge, with Plasmodium falciparum accounting for approximately 50% of cases and posing a considerable threat. Despite advances in control measures, malaria continues to cause an estimated one million deaths annually. The complex lifecycle of P. falciparum, involving both vertebrate hosts and Anopheles mosquitoes, complicates eradication efforts. The parasites resistance to existing antimalarial drugs, along with medication toxicity, necessitates innovative therapeutic approaches. Recent research has revealed that harmine, an alkaloid produced by an endophytic gut bacterium of Anopheles mosquitoes, can impede the transmission of the malarial parasite to humans by inhibiting a crucial life stage. This study investigates harmala alkaloids, sourced from plants and bacteria such as Peganum harmala, as potential alternatives to conventional antimalarial drugs. Notably, harmine and harmaline have shown promising antimalarial activity by inhibiting the essential enzyme protein kinase 4 (PK4), which is vital for the parasites survival. These compounds exhibit lower toxicity, effectively inhibiting both the blood stage growth and transmission of the parasite. Using in silico methodologies, including ADME analysis, molecular docking, MD simulation, and toxicity analysis, this study identifies harmala alkaloids as potential inhibitors against crucial P. falciparum proteins. Targeting proteins essential for the parasites survival, similar to established drugs like pfCRT protein, lays the foundation for developing effective antimalarial treatments. The comprehensive screening of harmala alkaloid molecules opens avenues for the pharmaceutical industry to tackle challenges related to drug resistance and toxicity, offering a promising route for the biorational management of malaria.

bioinformatics↗

bioRxiv2022

Subtractive proteomics analysis to uncover the potent drug targets for distinctive drug design of Candida auris

Candida auris is a serious health concern of current world that possess serious global health threat and is emerging at a high rate. Available antifungal drugs are failing to combat this pathogen as they are growing resistance toward those drugs and some strains have already showed resistant to all three available antifungal drugs in the market. Finding alternative treatments is a must, therefore, to save lives from this foe. To make the way easier for developing new treatments, we have made some insilico analysis of this pathogen to identify suitable targets for designing drugs and also suggested some potential metabolites to test in vivo condition after some computational analysis. After the subtraction of duplicate, non-essential, human homologs, non-metabolic, human microbiome similar and druggable proteins we ended up with three proteins (XP_028890156.1, XP_028891672.1 and XP_028891858.1) from a total of 5441 C. auris proteins. Blocking those proteins will result in the destruction of the pathogen while the host will remain safe from unintentional blocking. Their subcellular locations and interaction with high number of proteins also indicate their suitability as drug target candidates. After analyzing in silico docking of 29 potential antifungal from plant origin with those three proteins we selected Caledonixanthone E, Viniferin, Glaucine, Jatrorrhizine as the most potent weapon to block those proteins as they showed higher binding affinity. Furthermore, they were predicted to be safe and also showed proper ADME properties (Figure 1). O_FIG O_LINKSMALLFIG WIDTH=179 HEIGHT=200 SRC="FIGDIR/small/487516v1_fig1.gif" ALT="Figure 1"> View larger version (30K): org.highwire.dtl.DTLVardef@5ac4bcorg.highwire.dtl.DTLVardef@12a4b3eorg.highwire.dtl.DTLVardef@1b1d825org.highwire.dtl.DTLVardef@e581b3_HPS_FORMAT_FIGEXP M_FIG O_FLOATNOFigure 1:C_FLOATNO Schematic pipeline of the process C_FIG

bioinformatics↗