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UNIVERSITY OF BUCHAREST
FACULTY OF PHYSICS Guest
2024-11-24 11:45 |
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Conference: Bucharest University Faculty of Physics 2021 Meeting
Section: Biophysics; Medical Physics
Title:
Bovine serum albumin properties in the presence of rutin
Authors:
Alexa CREȚU, Nicoleta SANDU, Claudia CHILOM
*
Affiliation:
Department of Electricity, Solid Physics and Biophysics, Faculty of Physics, University of Bucharest, Măgurele, Romania
E-mail
cretualexa99@yahoo.com
Keywords:
BSA, rutin, quenching mechanism, FRET, denaturation
Abstract:
Bovine serum albumin (BSA) is the most abundant globular protein in the circulatory system. In the biomedical field, BSA is mainly used as carrier protein for small molecules and drugs, due to the long half-life, preferential accumulation in tumor tissue as a result of the enhanced permeability and retention effect and due to the ability to cross the blood-brain barrier. The drugs used for chemoterapy bind to BSA in three ways: covalent, non-covalent and as nanoparticle formulations [1].
Rutin is a flavonoid in the flavonol category, found in fruits, vegetables, tea and wine. It is a highly potent molecule obtained from the process of glycosylation of quercetin that has various medical, pharmaceutical and biological activities such as hepatoprotective, cardioprotective and antidiabetic activity [2]. Rutin acts as a strong antioxidant agent, by neutralizing free radicals and preventing lipid peroxidation. It has anti-inflammatory, anticancer and antibacterial properties. Rutin can cross the blood-brain barrier and fight neuroinflammation, being a very effective compound for treating neurodegenerative diseases, such as Alzheimer's and Parkinson’s disease.
The aim of this study was to assess the physico-chemical properties of BSA, its stability under the action of temperature and urea and the changes induced by rutin in the conformational stability of the protein. The spectroscopic techniques used were fluorescence spectroscopy and Förster resonance energy transfer (FRET). For both thermal and chemical denaturation, the fluorescence quenching was observed. Using van't Hoff representation, the thermodynamic parameters that characterize the process of thermal denaturation, such as entropy and enthalpy variation and the melting point for apo-BSA and BSA in the presence of rutin were determined. The distance between the two fluorophores and the efficiency of the energy transfer between the BSA and rutin were evaluated based on FRET.
References:
[1] Hoogenboezem E. N., Duvall C. L., Harnessing albumin as a carrier for cancer therapies, Advanced Drug Delivery Reviews, 130, 73 - 89, 2018, DOI:10.1016/j.addr.2018.07.011
[2] Ganeshpurkar A., Saluja A. K.,The Pharmacological Potential of Rutin, Saudi Pharm. J., 25(2), 149-164, 2017, DOI:10.1016/j.jsps.2016.04.025
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