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- Title
Combined Multispectroscopic and Molecular Docking Assessments to the Effect of an Anticonvulsant, Oxcarbazepine on Human Serum Albumin Conformation and its Binding Properties.
- Authors
Manjushree, M.; Revanasiddappa, H. D.
- Abstract
Elimination and distribution of drugs are affected by human serum albumin (HSA) interaction. In children and adults, specific types of seizures are controlled by oxcarbazepine (OXZ) alone or in combination with other medications. However, the OXZ interaction with HSA was probed through 3D fluorescence, emission fluorescence, UV-Vis spectroscopy, and molecular docking. OXZ statically quenched the HSA fluorescence spontaneously and exothermically. Thermodynamic parameters revealed the involvement of hydrogen bonds together with van der Waals forces. Molecular docking inspections confirmed that OXZ is bound to site I of HSA. Strong binding with OXZ (of Kb order 105 L/mol) reduced the secondary, micro-environmental, and conformational structures of HSA, suggesting that it unfolds. Thus, the assessment of such conformational details of OXZ–HSA binding is pivotal in surveying the efficacy of OXZ as a therapeutic operator and interpreting its pharmacokinetic properties.
- Subjects
SERUM albumin; PHENOBARBITAL; VAN der Waals forces
- Publication
Journal of Applied Spectroscopy, 2022, Vol 89, Issue 2, p350
- ISSN
0021-9037
- Publication type
Article
- DOI
10.1007/s10812-022-01365-x