دورية أكاديمية
Surface plasmon resonance and molecular docking studies of bovine serum albumin interaction with neomycin: kinetic and thermodynamic analysis
| العنوان: | Surface plasmon resonance and molecular docking studies of bovine serum albumin interaction with neomycin: kinetic and thermodynamic analysis |
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| المؤلفون: | Maryam Sharifi, Jafar Ezzati Nazhad Dolatabadi, Farzaneh Fathi, Mostafa Zakariazadeh, Abolfazl Barzegar, Mohammad Rashidi, Habib Tajalli, Mohammad-Reza Rashidi |
| المصدر: | BioImpacts, Vol 7, Iss 2, Pp 91-97 (2017) |
| بيانات النشر: | Tabriz University of Medical Sciences, 2017. |
| سنة النشر: | 2017 |
| المجموعة: | LCC:Medicine (General) LCC:Biology (General) |
| مصطلحات موضوعية: | Enthalpy, Entropy, Equilibrium constants (KD), Surface plasmon resonance, Thermodynamic, Medicine (General), R5-920, Biology (General), QH301-705.5 |
| الوصف: | Introduction: The interactions between biomacromolecules such as serum albumin (SA) and various drugs have attracted increasing research attention in recent years. However, the study of SA with those drugs that have relatively high hydrophilicity and a lower affinity for SA could be a challenging issue. At the present study, the interaction of bovine SA (BSA) with neomycin as a hydrophilic drug has been investigated using surface plasmon resonance (SPR) and molecular docking methods. Methods: BSA was immobilized on the carboxymethyl dextran hydrogel sensor chip after activation of carboxylic groups through NHS/EDC and, then, the neomycin interaction with BSA at different concentrations (1-128 µM) was investigated. Results: Dose-response sensorgrams of BSA upon increasing concentration of neomycin has been shown through SPR analysis. The small KD value (4.96 e-7 at 40°C) demonstrated high affinity of neomycin to BSA. Thermodynamic parameters were calculated through van’t Hoff equation at 4 different temperatures. The results showed that neomycin interacts with BSA via Van der Waals interactions and hydrogen bonds and increase of KD with temperature rising indicated that the binding process was entropy driven. Molecular docking study confirmed that hydrogen bond was the major intermolecular force stabilizing neomycin-BSA complex. Conclusion: The attained results showed that neomycin molecules can efficiently distribute within the body after interaction with BSA in spite of having hydrophilic properties. Besides, SPR can be considered as a useful instrument for study of the interaction of hydrophilic drugs with SA. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English |
| تدمد: | 2228-5660 2228-5652 |
| Relation: | http://bi.tbzmed.ac.ir/PDF/bi-7-91.pdf; https://doaj.org/toc/2228-5660; https://doaj.org/toc/2228-5652 |
| DOI: | 10.15171/bi.2017.12 |
| URL الوصول: | https://doaj.org/article/e48a377a1a0f4199a2a4fac3bf798a2b |
| رقم الأكسشن: | edsdoj.48a377a1a0f4199a2a4fac3bf798a2b |
| قاعدة البيانات: | Directory of Open Access Journals |
Full Text Finder | تدمد: | 22285660 22285652 |
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| DOI: | 10.15171/bi.2017.12 |