Mode of encapsulation of Linezolid by β-Cyclodextrin and its role in bovine serum albumin binding
| Autor: | N. Sudha, Israel V.M.V.E., Sowrirajan Chandrasekaran, Y. Sameena |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
Polymers and Plastics
Stereochemistry Nuclear Overhauser effect chemistry.chemical_compound Anti-Infective Agents Amide Acetamides polycyclic compounds Materials Chemistry heterocyclic compounds Bovine serum albumin Oxazolidinones Protein Synthesis Inhibitors chemistry.chemical_classification Quenching (fluorescence) Cyclodextrin biology beta-Cyclodextrins Organic Chemistry Linezolid Serum Albumin Bovine biochemical phenomena metabolism and nutrition bacterial infections and mycoses Fluorescence Binding constant Molecular Docking Simulation carbohydrates (lipids) Crystallography Spectrometry Fluorescence Förster resonance energy transfer chemistry biology.protein Spectrophotometry Ultraviolet |
| Zdroj: | Carbohydrate Polymers. 115:589-597 |
| ISSN: | 0144-8617 |
| DOI: | 10.1016/j.carbpol.2014.09.022 |
| Popis: | We describe, in this article, the associative interaction between Linezolid and β-Cyclodextrin, and the influence of β-Cyclodextrin on Linezolid's binding to Bovine serum albumin. β-Cyclodextrin forms a 1:1 inclusion complex with Linezolid, with a binding constant value of 3.51 × 102 M−1. The binding is studied using ultraviolet–visible absorption, fluorescence, nuclear magnetic resonance, and rotating-frame overhauser effect spectroscopic techniques. The amide substituent on the oxazolidinone ring of Linezolid is involved in its binding to β-Cyclodextrin. The binding of the Linezolid to bovine serum albumin, in the absence and the presence of β-Cyclodextrin, is studied by analyzing the fluorescence quenching and Forster resonance energy transfer. The Stern–Volmer quenching constant, the binding constant, and energy transfer occurring on the interaction of the Linezolid with BSA are found to be smaller in the presence of β-Cyclodextrin than in water. |
| Databáze: | OpenAIRE |
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