THz spectroscopic fingerprints of the hydration upon globular protein assembly
Year: 2026
Authors: Caminiti L., Nalige S.S., Torre R., Havenith M.
Autors Affiliation: Univ Florence, Dept Phys & Astron, Sesto Fiorentino, FI, Italy; European Lab Nonlinear Spect, Sesto Fiorentino, FI, Italy; Ruhr Univ Bochum, Dept Phys Chem 2, D-44801 Bochum, Germany; CNR, Ist Nazl Ott, Sesto Fiorentino, FI, Italy.
Abstract: Lysozyme is a well-known globular protein that can form self-assembled clusters. Here, we report the results of a study on the changes in solvation dynamics upon increasing protein concentration via THz spectroscopy. We find spectral solvation fingerprints in the THz frequency range, which are clearly distinguished from those for liquid-liquid phase separation or liquid-solid phase separation. Furthermore, we carried out supplementary measurements using dynamic light scattering to characterize the size distribution of the protein clusters. This study sheds light on using THz studies of solvation dynamics to characterize and differentiate protein hydration in the case of protein assembly, liquid-liquid phase separation, and liquid-solid phase separation.
Journal/Review: JOURNAL OF CHEMICAL PHYSICS
Volume: 164 (13) Pages from: 134907-1 to: 134907-5
More Information: This work was funded by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) under Germany’s Excellence Strategy, Grant No. EXC2033-390677874-RESOLV (M.H.), and Next Generation EU Program: Project PRIN-2022JWAF7Y (CUP:B53D230-04250006) and I-PHOQS Infrastructure (Grant Nos. IR0000016 and ID D2B8D520, CUP:B53C22001750006) and Project CNR-FOE-LENS (R.T.). S.N. acknowledges support funded by the Deutsche Forschungsgemeinschaft (DFG) under Grant No. GRK2376/331085229.KeyWords: Liquid-liquid; Equilibrium Clusters; LysozymeDOI: 10.1063/5.0310494
