Calorimetry and FTIR reveal the ability of URG7 protein to modify the aggregation state of both cell lysate and amylogenic α-synuclein - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue AIMS Biophysics Année : 2020

Calorimetry and FTIR reveal the ability of URG7 protein to modify the aggregation state of both cell lysate and amylogenic α-synuclein

Résumé

Differential scanning calorimetry and FITR analyses allowed to investigate the role of URG7 (up-regulated gene clone 7) protein involved in the development of hepatocellular carcinoma induced by hepatitis B virus infection, on the physical structure both of lysates of human hepatoblastoma cells (HepG2) stressed with tunicamycin and α-synuclein, one of the proteins associated with neurogenerative diseases. The protein-water interfacial region was identified and correlated with protein structure. DSC results confirm through the interfacial water behavior that URG7 is able to act in two ways: it maintains the interfacial water stability and controls the mobile fraction level, thereby the flexibility and the protein folding. The mobile water phase increases strongly for cells exposed to α-synuclein, demonstrating an important influence on water hydration. FTIR results evidenced an increase of about 30% of cross β structures in cells exposed to α-synuclein, associated with aggregated proteins. In stress conditions, URG7 was able to maintain the same fraction of mobile water as untreated cells. URG7 was able to restore the water reorientation ability around the complex lysate system and reduced abnormal protein folding.
Fichier principal
Vignette du fichier
Dandurand_26440.pdf (1.23 Mo) Télécharger le fichier
Origine : Fichiers éditeurs autorisés sur une archive ouverte
Loading...

Dates et versions

hal-02906200 , version 1 (24-07-2020)

Identifiants

Citer

Jany Dandurand, Angela Ostuni, Maria Francesca Armentano, Maria Antonietta Crudele, Vincenza Dolce, et al.. Calorimetry and FTIR reveal the ability of URG7 protein to modify the aggregation state of both cell lysate and amylogenic α-synuclein. AIMS Biophysics, 2020, 7 (3), pp.189-203. ⟨10.3934/biophy.2020015⟩. ⟨hal-02906200⟩
84 Consultations
95 Téléchargements

Altmetric

Partager

Gmail Facebook X LinkedIn More