title: Resveratrol induces thermal stabilization of human serum albumin and modulates the early aggregation stage.
abstract: Several phenolic compounds bind to proteins and show the ability to interfere with their aggregation process. The impact of the natural polyphenol resveratrol on the stability and heat induced aggregation of human serum albumin (HSA) was investigated by differential scanning calorimetry (DSC), attenuated total reflectance Fourier transform infrared (ATR-FTIR), UV-vis absorbance, ThT fluorescence, atomic force microscopy (AFM) and molecular modeling. The binding of resveratrol to HSA improves the stability of the protein to thermal unfolding, particularly for the energetic domain containing the ligand binding site, as modeled by computational techniques. The thermal unfolding is irreversible and after the melting the protein aggregates, either with or without the ligand. The kinetics of HSA aggregation between 70 and 80°C shows an exponential growth of the absorbance change and it slows down when resveratrol is added. The aggregates have fibril-like morphology and resveratrol attenuates the formation of β-structured species. The overall results suggest that resveratrol stabilizes the protein structure and modulates the formation of fibrils along the initial stage of the HSA aggregation pathway.
authors: Molecular Biophysics Laboratory, Department of Physics, University of Calabria, 87036 Rende, Italy.
authors: Andrea
authors: A
authors: Stirpe
authors: Molecular Biophysics Laboratory, Department of Physics, University of Calabria, 87036 Rende, Italy.
authors: Manuela
authors: M
authors: Pantusa
authors: Licryl Laboratory, CNR-NANOTEC and CEMIF.Cal, Department of Physics, University of Calabria, 87036 Rende, Italy.
authors: Bruno
authors: B
authors: Rizzuti
authors: Department of Physics, University of Calabria, 87036 Rende, Italy; Licryl Laboratory, CNR-NANOTEC and CEMIF.Cal, Department of Physics, University of Calabria, 87036 Rende, Italy.
authors: Maria P
authors: MP
authors: De Santo
authors: Molecular Biophysics Laboratory, Department of Physics, University of Calabria, 87036 Rende, Italy; CNISM, UdR Cosenza, 87036 Rende, Italy.
authors: Luigi
authors: L
authors: Sportelli
authors: Molecular Biophysics Laboratory, Department of Physics, University of Calabria, 87036 Rende, Italy; CNISM, UdR Cosenza, 87036 Rende, Italy.
authors: Rosa
authors: R
authors: Bartucci
authors: Molecular Biophysics Laboratory, Department of Physics, University of Calabria, 87036 Rende, Italy; CNISM, UdR Cosenza, 87036 Rende, Italy. Electronic address: rita.guzzi@fis.unical.it.
authors: Rita
authors: R
authors: Guzzi
mesh_terms: D001665:Binding Sites; D006358:Hot Temperature; D006801:Humans; D007700:Kinetics; D066329:Protein Aggregates; D011485:Protein Binding; D000072417:Protein Domains; D055550:Protein Stability; D017433:Protein Structure, Secondary; D058767:Protein Unfolding; D000077185:Resveratrol; D012709:Serum Albumin / Q000737:chemistry*; D013267:Stilbenes / Q000737:chemistry*; D013816:Thermodynamics
chemical_list: D066329:Protein Aggregates; D012709:Serum Albumin; D013267:Stilbenes; D000077185:Resveratrol
keywords: AFM; ATR-FTIR; Calorimetry; Human serum albumin; Resveratrol; Thermal aggregation