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Discrete SeNPs-Macromolecule Binding Manipulated by Hydrophilic Interaction.
Amol V Pansare1, Amol A Shedge1, Vishwanath R Patil1
1Department of Chemistry, University of Mumbai, Santacruz (E), Mumbai, 400098, India.
International Journal of Biological Macromolecules
|October 17, 2017
Summary
Selenium nanoparticles (SeNPs) stabilize Bovine Serum Albumin (BSA) structure through hydrophilic interactions, enhancing its stability and potentially aiding drug delivery systems.
Area of Science:
- Biomaterials Science
- Nanotechnology
- Biochemistry
Background:
- Nanoparticle-protein conjugates are crucial for biological diagnostics and nanotechnology.
- Understanding protein-nanoparticle interactions is key to developing advanced applications.
Purpose of the Study:
- To investigate the interaction between selenium nanoparticles (SeNPs) and Bovine Serum Albumin (BSA).
- To explore the effects of SeNPs on BSA stability, conformation, and esterase-like activity.
- To determine the binding forces and site of interaction between SeNPs and BSA.
Main Methods:
- UV-Vis spectroscopy
- Fluorescence spectroscopy
- Circular Dichroism (CD) spectroscopy
- Thermal denaturation studies
- Investigation of BSA esterase-like activity towards PNPA
Main Results:
- SeNPs interact with BSA via physical adsorption, primarily through hydrophilic bonding.
- Binding of SeNPs induces conformational changes in BSA's secondary structure.
- SeNPs act as a stabilizing agent for BSA, confirmed by thermal denaturation.
- The binding site of SeNPs on BSA is located near Sudlow's site II.
- SeNPs did not significantly alter the esterase-like activity of BSA.
Conclusions:
- SeNPs stabilize BSA structure and influence its conformation through hydrophilic interactions.
- The BSA-SeNPs complex formation is governed by hydrophilic forces.
- These findings suggest potential applications for SeNP-BSA conjugates in drug delivery systems.