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Luminophore Formation in Various Conformations of Bovine Serum Albumin by Binding of GoldIII
Published on: August 31, 2018
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Interactions between gold nanoparticles with different morphologies and human serum albumin
Jiahui Dai1, Chao Chen1, Man Yin1
1Clinical Medical College, Jining Medical University, Jining, Shandong, China.
Frontiers in Chemistry
|November 6, 2023
Summary
Gold nanoparticles (AuNPs) with varied shapes interact with human serum albumin (HSA), causing fluorescence quenching and conformational changes. Nanoflowers (AuNFs) showed the strongest binding and least conformational change with HSA.
Area of Science:
- Nanomaterials Science
- Biochemistry
- Spectroscopy
Background:
- Gold nanoparticles (AuNPs) are increasingly explored for biomedical applications.
- Understanding nanoparticle-protein interactions is crucial for drug delivery and biocompatibility.
- Human serum albumin (HSA) is a key protein in biological systems, often interacting with nanomaterials.
Purpose of the Study:
- To synthesize and characterize gold nanoparticles (AuNPs) with three distinct morphologies: nanospheres (AuNSs), nanorods (AuNRs), and nanoflowers (AuNFs).
- To investigate the interactions between these different AuNP shapes and human serum albumin (HSA).
- To compare the binding affinities, thermodynamic parameters, and conformational changes induced in HSA by the various AuNP morphologies.
Main Methods:
- Synthesis of AuNPs (AuNSs, AuNRs, AuNFs) using a seeding method.
- Characterization via UV-vis spectroscopy, Transmission Electron Microscopy (TEM), Dynamic Light Scattering (DLS), Zeta potential, Circular Dichroism (CD), and Fourier Transform Infrared Spectroscopy (FTIR).
- Fluorescence quenching experiments and variable-temperature fluorescence spectroscopy to determine binding constants, thermodynamic parameters, and quenching mechanisms.
Main Results:
- All three AuNP morphologies exhibited concentration-dependent fluorescence quenching of HSA, indicating static quenching interactions.
- Thermodynamic analysis revealed spontaneous interactions (Gibbs free energy < 0) between AuNPs and HSA.
- Gold nanoflowers (AuNFs) demonstrated the strongest binding affinity to HSA, while all AuNP shapes induced a reduction in HSA's α-helix content, with AuNFs causing the least conformational change.
Conclusions:
- Different AuNP shapes exhibit varying interaction strengths and conformational effects on HSA.
- AuNFs show favorable interactions with HSA, suggesting potential for targeted drug delivery applications.
- These findings provide valuable insights into nanoparticle-protein interactions for future nanomedicine development.
