Temperature-induced β-aggregation of fibronectin in aqueous solution

• Published in: Biochimica et biophysica acta 2002-05, Vol.1597 (1), p.12-21
• Main Authors: Pauthe, E, Pelta, J, Patel, S, Lairez, D, Goubard, F
• Format: Article
• Language: English
• Subjects: Fibronectin; Fibronectins - chemistry; Fourier-transform infrared; Humans; Protein Conformation; Protein Structure, Secondary; Scattering, Radiation; Solutions; Spectrometry, Fluorescence; Spectroscopy, Fourier Transform Infrared; Temperature; Water; β-Aggregation
• ISSN: 0167-4838; 0006-3002; 1879-2588
• DOI: 10.1016/S0167-4838(02)00271-6

Fibronectin structural reorganization induced by temperature has been investigated by Fourier-transform infrared (FT-IR) spectroscopy and light-scattering experiments. At 20 °C, from resolution enhanced by FT-IR spectra, 43% of β sheet, 31% of turn and 26% of unordered structures were estimated. Static and quasi-elastic light-scattering results do not change significantly between 20 and 34 °C. Just below 50 °C, a decrease of 1/3 of β sheet structures contents is observed, concomitantly with a corresponding increase of turn. The contribution of disordered structures is found to be temperature-independent. Above 50 °C, our data reveals the formation of intermolecular hydrogen bonding leading to the formation of intermolecular β sheet structures. The IR band absorption at 1618 cm −1 increases strongly as a function of temperature. The scattered intensity increases and becomes strongly q 2-dependent. The dynamic structure factor is not a single exponential decay and becomes strongly dependent on the scattering angle. These results demonstrate that aggregation occurs in fibronectin solution. When temperature decreases, this aggregation is found irreversible. Fibronectin aggregation is driven by the formation of intermolecular hydrogen bonds responsible for intermolecular β sheet structures.