M
Mallika Pathak
Researcher at Miranda House, University of Delhi
Publications - 29
Citations - 450
Mallika Pathak is an academic researcher from Miranda House, University of Delhi. The author has contributed to research in topics: Bovine serum albumin & Quenching (fluorescence). The author has an hindex of 9, co-authored 25 publications receiving 302 citations. Previous affiliations of Mallika Pathak include University of Delhi.
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Synthesis, characterization of 1,2,4-triazole Schiff base derived 3d-metal complexes: Induces cytotoxicity in HepG2, MCF-7 cell line, BSA binding fluorescence and DFT study.
TL;DR: Result indicates that metal complexes shows increase cytotoxicity in proliferation to cell lines as compared to free ligand.
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Spectroscopic and molecular modelling studies of binding mechanism of metformin with bovine serum albumin
Deepti Sharma,Himanshu Ojha,Mallika Pathak,Bhawna Singh,Navneet Sharma,Anju Singh,Rita Kakkar,Rakesh Sharma +7 more
TL;DR: The data suggested the existence of non-covalent specific binding interaction in the complexation of meetformin with BSA, which will certainly contribute to the development of metformin as a therapeutic molecule.
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Binding of ethyl pyruvate to bovine serum albumin: Calorimetric, spectroscopic and molecular docking studies
Mallika Pathak,Rashmi Mishra,Paban K. Agarwala,Himanshu Ojha,Bhawna Singh,Anju Singh,Shrikant Kukreti +6 more
TL;DR: The binding mechanism of the ethyl pyruvate with bovine serum albumin was investigated using UV–vis absorption, fluorescence, circular dichroism, isothermal titration calorimetry and molecular docking techniques and results will definitely contribute to the development of ethylpyruvates as drug.
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A DFT study of the structures of pyruvic acid isomers and their decarboxylation.
TL;DR: Pyruvic acid and its isomers, including the enol tautomers and enantiomeric lactone structures, have been investigated at the B3LYP/6-311 + + G(3df,3pd) level, and it is found that a keto form is the most stable, with one methyl hydrogen in a synperiplanar position with respect to the keto oxygen, which agrees with previous theoretical and experimental determinations.
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Spectroscopic and molecular modelling study of binding mechanism of bovine serum albumin with phosmet
Afreen Jahan Rahman,Deepti Sharma,Deepanshu Kumar,Mallika Pathak,Anju Singh,Vinod Kumar,Raman Chawla,Himanshu Ojha +7 more
TL;DR: The binding interactions of phosmet with bovine serum albumin (BSA) was investigated to determine the free concentration ofphosmet for its neurotoxicity and displayed that non-covalent interactions played a significant role in the binding mechanism.