Sarveswari Sundaramoorthy

Dr. Sarveswari Sundaramoorthy


Research Focus & Metrics

Academic Career Length

15Years (2012-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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22 August 2025 in RSC Advances
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NCNagesh Dhanaji Chavan
Nagesh Dhanaji Chavan
SSSarveswari Sundaramoorthy
Sarveswari Sundaramoorthy
Vijayakumar VijayaparthasarathiVijayakumar Vijayaparthasarathi
Vijayakumar Vijayaparthasarathi
Quinoline plays a crucial role in drug development and pharmaceutical synthesis. This review highlights quinoline-based medications and their therapeutic potential, especially for malaria and cancer, impacting millions worldwide.

6 April 2020 in ChemistrySelect
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RBR. Bhaskar
R. Bhaskar
SSSarveswari Sundaramoorthy
Sarveswari Sundaramoorthy
An efficient thiocarbohydrazide based fluorescencesensor S5 for the selective detection of Hg 2+ in semi‐aqueous medium has been successfully designed and synthesized. The absorption (UV‐Vis) and emission (fluorescence) properties of S5 were studied in various solvents. The sensor S5 displayed no distinct changes in absorption with various solvents; however some remarkable changes were noticed in fluorescence studies. Solvent dependent spectral characterization of S5 was explored via the Lippert‐Mataga plot. UV‐Vis and fluorescence studies also revealed that the sensor S5 could selectively detect Hg 2+ ion over the other tested metal ions. The interaction of S5 with Hg 2+ leads to colour change from colourless to yellow. The observed quenching in fluorescence intensity may be due to chelation enhanced fluorescence quenching (CHEQ). The sensing mechanism was arrived through DFT and 1 H NMR titration studies. The limit of detection was found to be 1.26 nM with a wide pH range of 4–10. Moreover, sensor S5 could demonstrate sensing efficiency for lower concentrations of Hg 2+ in real sample analysis. Its performance, as a test strip and in analysis of various water samples conferred its superior selectivity.

1 June 2020 in Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
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RBR. Bhaskar
R. Bhaskar
VVV. Vijayakumar
V. Vijayakumar
VSVenkatesan Srinivasadesikan
Venkatesan Srinivasadesikan
SLShyi-Long Lee
Shyi-Long Lee
SSSarveswari Sundaramoorthy
Sarveswari Sundaramoorthy

1 October 2016 in European Journal of Medicinal Chemistry
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PGPradip K. Gadekar
Pradip K. Gadekar
ARAbhijit Roychowdhury
Abhijit Roychowdhury
PKPrashant S. Kharkar
Prashant S. Kharkar
VKVijay M. Khedkar
Vijay M. Khedkar
MAManisha Arkile
Manisha Arkile
SSSarveswari Sundaramoorthy
Sarveswari Sundaramoorthy

20 September 2014 in Applied Biochemistry and Biotechnology
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SSSarveswari Sundaramoorthy
Sarveswari Sundaramoorthy
Vijayakumar VijayaparthasarathiVijayakumar Vijayaparthasarathi
Vijayakumar Vijayaparthasarathi
SRSiva Ramamoorthy
Siva Ramamoorthy
RPR. Priya
R. Priya

28 March 2024 in ACS Omega
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NLNarayanaswamy Lohitha
Narayanaswamy Lohitha
PKPeruru Hemanth Kumar
Peruru Hemanth Kumar
SSSarveswari Sundaramoorthy
Sarveswari Sundaramoorthy
SRSanket Rathod
Sanket Rathod
SCSomdatta Chaudhari
Somdatta Chaudhari
Vijayakumar VijayaparthasarathiVijayakumar Vijayaparthasarathi
Vijayakumar Vijayaparthasarathi
A series of novel 24 phenylhydrazono phenoxyquinoline derivatives were synthesized with moderate to excellent yield and screened for their efficacy against the α-amylase enzyme through in silico studies. The structures were characterized using spectroscopic techniques such as 1HNMR, 13CNMR, and HREI-MS. Comprehensive computational studies including, drug-likeness and ADMET profiling, quantum chemical calculations, molecular docking, and molecular dynamics (MD) simulation studies, were performed. A density functional theory study of the synthesized compounds indicated a favorable reactivity profile. The synthesized novel analogues were docked against α-amylase (PDB 6OCN) enzymes to investigate the binding interactions. Based on the docking studies, one of the compounds was found to be the hit with the highest negative binding affinity for α-amylase. A MD simulation study indicated stable binding throughout the simulation.