Multi-length scale structural investigation of lysozyme self-assembly
Year: 2022
Authors: Catalini S., Lutz-Bueno V., Usuelli M., Diener M., Taschin A., Bartolini P., Foggi P., Paolantoni M., Mezzenga R., Torre R.
Autors Affiliation: Univ Perugia, Dipartimento Fis & Geol, Via Alessandro Pascoli, I-06123 Perugia, Italy; Univ Firenze, European Lab Nonlinear Spect, Via Nello Carrara 1, I-50019 Sesto Fiorentino, Italy; Swiss Fed Inst Technol, LFO, Dept Hlth Sci & Technol, Schmelzbergstr 9, CH-8092 Zurich, Switzerland; ENEA Ctr Ric Frascati, Via E Fermi 45, I-00044 Frascati, Italy; Univ Firenze, Dipartimento Fis Astron, Via G Sansone 1, I-50019 Sesto Fiorentino, Italy; Univ Perugia, Dipartimento Chim Biol & Biotecnol, Via Elce Sotto 8, I-06123 Perugia, Italy; Swiss Fed Inst Technol, Dept Mat, Wolfgang Pauli Str 10, CH-8093 Zurich, Switzerland; Paul Scherrer Inst PSI, CH-5232 Villigen, Switzerland.
Abstract: Reactive amyloid oligomers are responsible for cytotoxicity in amyloid pathologies and because of their unstable nature characterizing their behavior is a challenge. The physics governing the self-assembly of proteins in crowded conditions is extremely complex and its comprehension, despite its paramount relevance to understanding molecular mechanisms inside cells and optimizing pharmaceutical processes, remains inconclusive. Here, we focus on the amyloid oligomerization process in self-crowded lysozyme aqueous solutions in acidic conditions. We reveal that the amyloid oligomers form at high protein concentration and low pH. Through multi-length scale spectroscopic investigations, we find that amyloid oligomers can further interconnect with each other by weak and non-specific interactions forming an extended network that leads to the percolation of the whole system. Our multi-length scale structural analysis follows the thermal history of amyloid oligomers from different perspectives and highlights the impact of hierarchical self-assembly of biological macromolecules on functional properties.
Journal/Review: ISCIENCE
Volume: 25 (7) Pages from: 104586-1 to: 104586-16
More Information: This research was funded by Ente Cassa di Risparmio di Firenze (prog. 2018.1042), Ministero dell’Istruzione dell’Universita e della Ricerca Italiano (PRIN2017-2017Z55KCW), European Union’s Horizon 2020 research and innovation program under grant agreement no 871124 Laserlab-Europe and the project CNR-FOE-LENS-2021.KeyWords: Egg-white Lysozyme; X-ray-scattering; Ultrasonic Spectroscopy; Cluster Formation; Amyloid Formation; Gelation; Ftir; Proteins; Aggregation; TemperatureDOI: 10.1016/j.isci.2022.104586ImpactFactor: 5.800Citations: 3data from “WEB OF SCIENCE” (of Thomson Reuters) are update at: 2024-11-24References taken from IsiWeb of Knowledge: (subscribers only)
