Resveratrol induces thermal stabilization of human serum albumin and modulates the early aggregation stage
| Autor: | Andrea Stirpe, Rita Guzzi, Rosa Bartucci, Bruno Rizzuti, Maria Penelope De Santo, Luigi Sportelli, Manuela Pantusa |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Hot Temperature Serum albumin Plasma protein binding Resveratrol Protein aggregation 010402 general chemistry 01 natural sciences Biochemistry Protein Structure Secondary Absorbance Protein Aggregates 03 medical and health sciences chemistry.chemical_compound Protein structure Protein Domains Structural Biology Stilbenes medicine Humans Molecular Biology Serum Albumin Protein Unfolding Binding Sites biology Protein Stability General Medicine Human serum albumin Ligand (biochemistry) 0104 chemical sciences Kinetics 030104 developmental biology chemistry biology.protein Biophysics Thermodynamics Protein Binding medicine.drug |
| Zdroj: | International Journal of Biological Macromolecules. 92:1049-1056 |
| ISSN: | 0141-8130 |
| DOI: | 10.1016/j.ijbiomac.2016.08.014 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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