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- W4286722222 abstract "Biomaterial protein, perform the most effectual and distinct functions in cells. They execute numerous functions that include control of biochemical reaction, transport of molecules, building the immune system etc. Considering the fact that proteins are the preferred druggable targets for most of small molecules/ligands; in this manuscript we have deciphered the thermodynamic profile of two antibiotic drugs sulfamethazine (SMZ) and sulfadiazine (SDZ) upon interaction with myoglobin. Temperature dependent fluorescence spectroscopy and molecular dynamic simulation have been employed to monitor the said complexation reaction(s). The experimental data denoted spontaneous, electrostatic and hydrophobic interaction involved between the protein and the drugs. The results further suggested enthalpy driven exothermic binding process for both the cases. The interaction affinity is slightly more for SMZ as compared to that SDZ. Molecular dynamics (MD) simulation complimented the complex bindings with stability and compactness of the protein upon ligation. This work can help and shape the study of biomaterial protein structure and function upon binding with the drug which will provide useful information in designing and modifying the target as well as the ligand in the field of biomedical research." @default.
- W4286722222 created "2022-07-23" @default.
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- W4286722222 date "2022-01-01" @default.
- W4286722222 modified "2023-09-26" @default.
- W4286722222 title "Molecular insight into sulfa antibiotic drug binding with human proteins" @default.
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- W4286722222 doi "https://doi.org/10.1016/j.matpr.2022.07.203" @default.
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