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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Mitra, Sivaprasad Sonu, Vikash K. Islam, Mullah Muhaiminul Moyon, N. Shaemningwar Gashnga, Pynsakhiat Miki |
| Description | Country affiliation: India Author Affiliation: Islam MM ( Centre for Advanced Studies, Department of Chemistry, North-Eastern Hill University, Shillong 793 022, India.); Sonu VK ( Centre for Advanced Studies, Department of Chemistry, North-Eastern Hill University, Shillong 793 022, India.); Gashnga PM ( Centre for Advanced Studies, Department of Chemistry, North-Eastern Hill University, Shillong 793 022, India.); Moyon NS ( Centre for Advanced Studies, Department of Chemistry, North-Eastern Hill University, Shillong 793 022, India.); Mitra S ( Centre for Advanced Studies, Department of Chemistry, North-Eastern Hill University, Shillong 793 022, India. Electronic address: smitra@nehu.ac.in.) |
| Abstract | The interaction and binding behavior of the well-known drug sulfadiazine (SDZ) and psychoactive stimulant caffeine (CAF) with human serum albumin (HSA) was monitored by in vitro fluorescence titration and molecular docking calculations under physiological condition. The quenching of protein fluorescence on addition of CAF is due to the formation of protein-drug complex in the ground state; whereas in case of SDZ, the experimental results were explained on the basis of sphere of action model. Although both these compounds bind preferentially in Sudlow's site 1 of the protein, the association constant is approximately two fold higher in case of SDZ (â ¼4.0×10(4)M(-1)) in comparison with CAF (â ¼9.3×10(2)M(-1)) and correlates well with physico-chemical properties like pKa and lipophilicity of the drugs. Temperature dependent fluorescence study reveals that both SDZ and CAF bind spontaneously with HSA. However, the binding of SDZ with the protein is mainly governed by the hydrophobic forces in contrast with that of CAF; where, the interaction is best explained in terms of electrostatic mechanism. Molecular docking calculation predicts the binding of these drugs in different location of sub-domain IIA in the protein structure. |
| ISSN | 13861425 |
| Volume Number | 152 |
| e-ISSN | 18733557 |
| Journal | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy |
| Language | English |
| Publisher | Elsevier |
| Publisher Date | 2016-01-05 |
| Publisher Place | Great Britain (UK) |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Anti-infective Agents Metabolism Caffeine Central Nervous System Stimulants Serum Albumin Sulfadiazine Binding Sites Fluorescence Humans Hydrophobic And Hydrophilic Interactions Molecular Docking Simulation Protein Binding Chemistry Static Electricity Thermodynamics Journal Article Research Support, Non-u.s. Gov't Discipline Spectroscopy |
| Content Type | Text |
| Resource Type | Article |
| Subject | Spectroscopy Atomic and Molecular Physics, and Optics Analytical Chemistry Instrumentation |
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