Modulation of protein-saccharide interactions by deep-sea osmolytes under high pressure stress.

Autor: Oliva R; Department of Chemical Sciences, University of Naples Federico II, Via Cintia 26, 80126 Naples, Italy. Electronic address: rosario.oliva2@unina.it., Ostermeier L; Department of Chemistry and Chemical Biology, Biophysical Chemistry, TU Dortmund University, Otto-Hahn-Str. 4a, 44227 Dortmund, Germany., Jaworek MW; Department of Chemistry and Chemical Biology, Biophysical Chemistry, TU Dortmund University, Otto-Hahn-Str. 4a, 44227 Dortmund, Germany., Del Vecchio P; Department of Chemical Sciences, University of Naples Federico II, Via Cintia 26, 80126 Naples, Italy., Gajardo-Parra N; Laboratory of Thermodynamics, Department of Biochemical and Chemical Engineering, TU Dortmund University, Emil-Figge-Str. 70, 44227 Dortmund, Germany., Cea-Klapp E; Departamento de Ingeniería Química, Faculty of Engineering, Universidad de Concepción, Concepción, Chile., Held C; Laboratory of Thermodynamics, Department of Biochemical and Chemical Engineering, TU Dortmund University, Emil-Figge-Str. 70, 44227 Dortmund, Germany., Petraccone L; Department of Chemical Sciences, University of Naples Federico II, Via Cintia 26, 80126 Naples, Italy., Winter R; Department of Chemistry and Chemical Biology, Biophysical Chemistry, TU Dortmund University, Otto-Hahn-Str. 4a, 44227 Dortmund, Germany. Electronic address: roland.winter@tu-dortmund.de.
Jazyk: angličtina
Zdroj: International journal of biological macromolecules [Int J Biol Macromol] 2024 Jan; Vol. 255, pp. 128119. Date of Electronic Publication: 2023 Nov 15.
DOI: 10.1016/j.ijbiomac.2023.128119
Abstrakt: Deep-sea organisms must cope with high hydrostatic pressures (HHP) up to the kbar regime to control their biomolecular processes. To alleviate the adverse effects of HHP on protein stability most organisms use high amounts of osmolytes. Little is known about the effects of these high concentrations on ligand binding. We studied the effect of the deep-sea osmolytes trimethylamine-N-oxide, glycine, and glycine betaine on the binding between lysozyme and the tri-saccharide NAG3, employing experimental and theoretical tools to reveal the combined effect of osmolytes and HHP on the conformational dynamics, hydration changes, and thermodynamics of the binding process. Due to their different chemical makeup, these cosolutes modulate the protein-sugar interaction in different ways, leading to significant changes in the binding constant and its pressure dependence. These findings suggest that deep-sea organisms may down- and up-regulate reactions in response to HHP stress by altering the concentration and type of the intracellular osmolyte.
Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
(Copyright © 2023 The Authors. Published by Elsevier B.V. All rights reserved.)
Databáze: MEDLINE
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