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UNIVERSITY OF BUCHAREST
FACULTY OF PHYSICS Guest
2024-11-21 16:36 |
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Conference: Bucharest University Faculty of Physics 2008 Meeting
Section: Electricity and Biophysics
Title:
Stability, structure and binding properties of human serum albumin
Authors:
Ioana Patrascu, Cristina Matei, Claudia Chilom and Aurel Popescu
Affiliation:
Department of Electricity and Biophysics, Faculty of Physics, University of Bucharest
E-mail
claudiafir@gmail.com
Keywords:
human serum albumin, absorption spectroscopy, fluorescence spectroscopy
Abstract:
At molecular level, details of conformation change, stability and ion binding of HSA are important keys for all processes in which this protein is involved. The experimental study has been carried out in order to investigate the structural modifications of HSA, identification of possible molecular partners and characterization of their interactions with HSA. The experiments of structure and the conformational modifications of HSA were performed in different pH conditions (from 4.5 to 12) in HEPES buffer, by absorption spectroscopy. All the experiments were carried out both in the absence and presence of calcium and magnesium ions. The information on the microenviroment exposure of the Trp residue (situated in the 214 position on the protein backbone) was obtained. We also have investigated the structural modifications induced by these ions on HSA, using fluorescence spectroscopy. Fluorescence technique is able to give information concerning temperature and pH influence on the HSA interaction with calcium and/or magnesium ions. The results show a net thermal denaturation of HSA, while the presence of calcium and magnesium ions, confer a thermal stability of HSA tertiary structure. HSA seems also to have a greater biological activity at basic pH as compared to the acidic one.
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