1. Biophysical Insight into the Interaction of Human Lysozyme with Anticancer Drug Anastrozole: A Multitechnique Approach
- Author
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Ali S. Abdelhameed, Fahad M. Almutairi, Rizwan Hasan Khan, Adel Ibrahim Al Alawy, and Mohammad Rehan Ajmal
- Subjects
Drug ,Technology ,Article Subject ,media_common.quotation_subject ,Science ,030303 biophysics ,Molecular Conformation ,Anastrozole ,Antineoplastic Agents ,Molecular Dynamics Simulation ,General Biochemistry, Genetics and Molecular Biology ,Structure-Activity Relationship ,03 medical and health sciences ,chemistry.chemical_compound ,Pharmacokinetics ,medicine ,Humans ,Molecule ,030304 developmental biology ,General Environmental Science ,media_common ,0303 health sciences ,Molecular Structure ,Chemistry ,Spectrum Analysis ,General Medicine ,Small molecule ,In vitro ,Transport protein ,Enzyme Activation ,Molecular Docking Simulation ,Biophysics ,Medicine ,Muramidase ,Lysozyme ,Research Article ,Protein Binding ,medicine.drug - Abstract
In the present study, we employ fluorescence spectroscopy, dynamic light scattering, and molecular docking methods. Binding of anticancer drug anastrozole with human lysozyme (HL) is studied. Binding of anastrozole to HL is moderate but spontaneous. There is anastrozole persuaded hydrodynamic change in HL, leading to molecular compaction. Binding of anastrozole to HL also decreased in vitro lytic activity of HL. Molecular docking results suggest the electrostatic interactions and van der Waals forces played key role in binding interaction of anastrozole near the catalytic site. Binding interaction of anastrozole to proteins other than major transport proteins in blood can significantly affect pharmacokinetics of this molecule. Hence, rationalizing drug dosage is important. This study also points to unrelated effects that small molecules bring in the body that are considerable and need thorough investigation.
- Published
- 2020