Richard Mariadasse, PhD
Postdoctoral AssociateAbout
Research
Publications
2026
Bio-carbon anchored praseodymium molybdate microflowers for sensitive detection of xanthine in biofluids and fish meat
Muthusamy K, Mariadasse R, Murugesan R, Rajendran K, Ganesan M, Madhuvilakku R, Piraman S, Gopalakrishnan G, Chang-Chien G. Bio-carbon anchored praseodymium molybdate microflowers for sensitive detection of xanthine in biofluids and fish meat. Journal Of The Taiwan Institute Of Chemical Engineers 2026, 183: 106641. DOI: 10.1016/j.jtice.2026.106641.Peer-Reviewed Original ResearchElectron-transfer kineticsGlassy carbon electrodeSensitive detectionDifferential pulse voltammetryElectroactive surface areaDetection of xanthineActive surface areaSurface areaLow detection limitHydrothermal-calcination routeCharge-transfer efficiencyBio-derived carbonComprehensive spectroscopic analysesPulse voltammetryElectrochemical interfaceCarbon electrodeHierarchical morphologyHydrothermal-calcinationExcellent stabilityLinear rangeHuman biofluidsDetection limitConventional electrodesSensing platformSpectroscopic analysisSynergistic Interface of dysprosium molybdate and Aloe Vera–derived carbon flakes enables ultrasensitive electrochemical detection of theophylline in food samples
Muthusamy K, Nallal M, Mariadasse R, Sekar K, Rajendran K, Ganesan M, Piraman S, Gopalakrishnan G, Chang-Chien G. Synergistic Interface of dysprosium molybdate and Aloe Vera–derived carbon flakes enables ultrasensitive electrochemical detection of theophylline in food samples. Microchemical Journal 2026, 221: 117033. DOI: 10.1016/j.microc.2026.117033.Peer-Reviewed Original ResearchX-ray photoelectron spectroscopyGlassy carbon electrodeField emission-scanning electron microscopyX-ray diffractionEnergy-dispersive X-ray spectroscopyElectrochemical detectionPresence of interfering speciesSynergistic interfaceUltrasensitive electrochemical detectionAbundant catalytic sitesX-raySensitive electrochemical sensorHydrothermal-calcination methodElectroactive surface areaResolution-transmission electron microscopyTwo-proton transfer mechanismSpiked real samplesStructurally similar alkaloidsUltralow detection limitDetermination of TPElectron microscopyElectrochemical studiesTP detectionCarbon electrodeElectrochemical sensorCrystal Structure of PH0140: Exogenous Amino Acids Induce Open Octameric Assembly Enables PromoterTTTT Binding for Transcription Regulation
Mariadasse R, Ahmad M, Pal R, Gurunathan K, Subramaniyan S, Biswal B, Muthuvel S, Thambusamy S, Jeyaraman J. Crystal Structure of PH0140: Exogenous Amino Acids Induce Open Octameric Assembly Enables PromoterTTTT Binding for Transcription Regulation. Journal Of Molecular Biology 2026, 438: 169664. PMID: 41633482, DOI: 10.1016/j.jmb.2026.169664.Peer-Reviewed Original ResearchConceptsEffector-binding domainFeast/famine regulatory proteinsTranscriptional regulationExogenous amino acidsExogenous isoleucineC-terminal loop regionB strandsExogenous tryptophanPyrococcus horikoshii OT3Amino acidsIsothermal titration calorimetryAmino acid bindingHypothetical proteinsDNA recognitionOctameric assemblyHomologous proteinsRegulatory proteinsPromoter fragmentLoop regionConformational openingAcid bindingOpen conformationRegulatory mechanismsStructural basisCrystal structure
2025
Targeting Catalytic Residues of TKTL1: A Multi‐Approach Study With Thiamine Analogs Combining QSAR, Pharmacophore Modeling, DFT, and Molecular Dynamics
Richard M, Subramaniyan S, Nagarajan H, Choubey S, Singla M, Biswal B, Jeyakanthan J. Targeting Catalytic Residues of TKTL1: A Multi‐Approach Study With Thiamine Analogs Combining QSAR, Pharmacophore Modeling, DFT, and Molecular Dynamics. ChemistrySelect 2025, 10 DOI: 10.1002/slct.202505619.Peer-Reviewed Original ResearchMolecular dynamicsCross-validated correlation coefficientQuantum mechanical calculationsBinding-free energySchiff base reactionPharmacophore hypothesisPharmacophore modelMechanical calculationsStable RMSDPool of compoundsCatalytic activityMM/PBSA analysisBase reactionCatalytic residuesActive site residuesBinding affinityPharmacophoreChemical reactionsCompoundsReactionPentose phosphate pathwaySite residuesCancer cellsInhibitory potentialThiamine analogsStrategic targeting of AckA in Mycobacterium tuberculosis using peptide inhibitors
Subramaniyan S, Nagarajan H, Mariadasse R, Vetrivel U, Jeyaraman J. Strategic targeting of AckA in Mycobacterium tuberculosis using peptide inhibitors. Archives Of Microbiology 2025, 207: 235. PMID: 40844623, DOI: 10.1007/s00203-025-04439-4.Peer-Reviewed Original ResearchConceptsMolecular dynamics simulationsFree energy landscapeMM/GBSA binding energy calculationsHydrogen bond formationAnti-tubercular agentsVirtual screeningBond formationEnergy calculationsComplex stabilityMM/PBSA analysisDynamics simulationsBinding interactionsStructural stabilityConformational stabilityPeptide dynamicsLow-energy basinsAnti-tubercular peptidesEnergy landscapeBinding affinitySimulation trajectoriesMultidrug resistancePhysicochemical propertiesMetabolism of Mycobacterium tuberculosisLead peptidePeptide inhibitor
2023
Integrated spectroscopic and MD simulation approach to decipher the effect of pH on the structure function of Staphylococcus aureus thymidine kinase
Ashraf A, Ahmad M, Mariadasse R, Khan M, Noor S, Islam A, Hassan I. Integrated spectroscopic and MD simulation approach to decipher the effect of pH on the structure function of Staphylococcus aureus thymidine kinase. Journal Of Biomolecular Structure And Dynamics 2023, 43: 1969-1980. PMID: 38100604, DOI: 10.1080/07391102.2023.2293270.Peer-Reviewed Original ResearchConceptsConformational dynamicsTertiary structureThymidine kinasePhosphorylation of thymidineDevelopment of effective inhibitorsPyrimidine salvage pathwayResistance to antibioticsEnzyme activity assaysRamaswamy H. SarmaEnzyme activity studiesHuman pathogensTK proteinSalvage pathwayDevelopment of therapeutic strategiesKinase activityEnzymatic activityDNA synthesisActivity assayKinaseCellular targetsMD simulation approachFunctional activityEnzymeClinical infectionActivity of TKStructural snapshots of Mycobacterium tuberculosis enolase reveal dual mode of 2PG binding and its implication in enzyme catalysis
Ahmad M, Jha B, Bose S, Tiwari S, Dwivedy A, Kar D, Pal R, Mariadasse R, Parish T, Jeyakanthan J, Vinothkumar K, Biswal B. Structural snapshots of Mycobacterium tuberculosis enolase reveal dual mode of 2PG binding and its implication in enzyme catalysis. IUCrJ 2023, 10: 738-753. PMID: 37860976, PMCID: PMC10619443, DOI: 10.1107/s2052252523008485.Peer-Reviewed Original ResearchConceptsStructural snapshotsActive siteBinding free energy calculationsGlycolytic pathwayConversion of 2-phosphoglycerateMetal ion coordinationHydrogen bonding interactionsActive-site loopMolecular dynamics studyFree energy calculationsReversible conversionDomains of lifeIon coordinationBinding posesEnergy calculationsAlternative conformationsPhosphoenolpyruvateEnzyme catalysisCanonical conformationReverse reactionConformationConformational changesDynamics studiesCatalysisProduct releaseStructural snapshots of Mycobacterium tuberculosis enolase reveal dual mode of 2PG binding and its implication in enzyme catalysis
Ahmad, M., Jha, B., Bose, S., Tiwari, S., Dwivedy, A., Kar, D., Pal, R., Mariadasse, R., Parish, T., Jeyakanthan, J. et al. (2024). IUCrJ 11, https://doi.org/10.1107/S2052252523008485.Peer-Reviewed Original Research
2022
Repurposing of Doxycycline to Hinder the Viral Replication of SARS-CoV-2: From in silico to in vitro Validation
Alexpandi R, Gendrot M, Abirami G, Delandre O, Fonta I, Mosnier J, Mariadasse R, Jeyakanthan J, Pandian S, Pradines B, Ravi A. Repurposing of Doxycycline to Hinder the Viral Replication of SARS-CoV-2: From in silico to in vitro Validation. Frontiers In Microbiology 2022, 13: 757418. PMID: 35602049, PMCID: PMC9115549, DOI: 10.3389/fmicb.2022.757418.Peer-Reviewed Original ResearchSARS-CoV-2 RdRpCatalytic domainNucleotide triphosphatesSARS-CoV-2 RNA-dependent RNA polymeraseRNA-dependent RNA polymeraseViral replicationRNA polymeraseViral entryStrains of SARS-CoV-2SARS-CoV-2Food and Drug AdministrationRdRpVariants of SARS-CoV-2Molecular mechanics Poisson-Boltzmann surface areaPoisson-Boltzmann surface areaCalculation of binding free energyDocking analysisEntry channelMolecular dynamics resultsRepurposing strategyAntiviral activityNucleotideHospitalized patientsTreatment efficacyDrug Administration
2021
Characterization of the NiRAN domain from RNA-dependent RNA polymerase provides insights into a potential therapeutic target against SARS-CoV-2
Dwivedy A, Mariadasse R, Ahmad M, Chakraborty S, Kar D, Tiwari S, Bhattacharyya S, Sonar S, Mani S, Tailor P, Majumdar T, Jeyakanthan J, Biswal B. Characterization of the NiRAN domain from RNA-dependent RNA polymerase provides insights into a potential therapeutic target against SARS-CoV-2. PLOS Computational Biology 2021, 17: e1009384. PMID: 34516563, PMCID: PMC8478224, DOI: 10.1371/journal.pcbi.1009384.Peer-Reviewed Original ResearchConceptsRNA-dependent RNA polymeraseNiRAN domainRNA polymeraseSARS-CoV-2 RdRpNucleotidyl transferase domainStructure of RdRpDomain active siteSARS-CoV-2-infected cellsAnti-microbial compoundsCOVID-19 pandemic urgencyIn silico toolsDomain organisationTransferase domainActive siteNucleoside triphosphatesNiRANThumb domainSARS-CoV-2Order NidoviralesRdRpBiochemical toolsDrug targetsKinaseInfected cellsTherapeutic target