Influence of Chemical Modifications of the Crystallophore on Protein Nucleating Properties and Supramolecular Interactions Network.

Autor: Roux A; Univ. Lyon, École Normale Supérieure de Lyon, CNRS UMR 5182, Laboratoire de Chimie, 46 allée d'Italie, 69007, Lyon, France.; Polyvalan SAS, Lyon, France., Alsalman Z; Univ Grenoble Alpes, CEA, CNRS, IBS, F-38000, Grenoble, France., Jiang T; Univ. Lyon, École Normale Supérieure de Lyon, CNRS UMR 5182, Laboratoire de Chimie, 46 allée d'Italie, 69007, Lyon, France., Mulatier JC; Univ. Lyon, École Normale Supérieure de Lyon, CNRS UMR 5182, Laboratoire de Chimie, 46 allée d'Italie, 69007, Lyon, France., Pitrat D; Univ. Lyon, École Normale Supérieure de Lyon, CNRS UMR 5182, Laboratoire de Chimie, 46 allée d'Italie, 69007, Lyon, France., Dumont E; Univ. Côte d'Azur, CNRS, Institut de Chimie de Nice, UMR 7272, 06108, Nice, France.; Institut Universitaire de France, 5 rue Descartes, 75005, Paris, France., Riobé F; Univ. Lyon, École Normale Supérieure de Lyon, CNRS UMR 5182, Laboratoire de Chimie, 46 allée d'Italie, 69007, Lyon, France.; Univ Bordeaux, Bordeaux INP, CNRS, Institut de Chimie de la Matière Condensée de Bordeaux, 33608, Pessac, France., Gillet N; Univ. Lyon, École Normale Supérieure de Lyon, CNRS UMR 5182, Laboratoire de Chimie, 46 allée d'Italie, 69007, Lyon, France., Girard E; Univ Grenoble Alpes, CEA, CNRS, IBS, F-38000, Grenoble, France., Maury O; Univ. Lyon, École Normale Supérieure de Lyon, CNRS UMR 5182, Laboratoire de Chimie, 46 allée d'Italie, 69007, Lyon, France.
Jazyk: angličtina
Zdroj: Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2024 Jul 05; Vol. 30 (38), pp. e202400900. Date of Electronic Publication: 2024 Jun 20.
DOI: 10.1002/chem.202400900
Abstrakt: Crystallophores are lanthanide complexes that have demonstrated outstanding induction of crystallization for various proteins. This article explores the effect of tailored modifications of the crystallophore first generation and their impact on the nucleating properties and protein crystal structures. Through high-throughput crystallization experiments and dataset analysis, we evaluated the effectiveness of these variants, in comparison to the first crystallophore generation G 1 . In particular, the V 1 variant, featuring a propanol pendant arm, demonstrated the ability to produce new crystallization conditions for the proteins tested (hen-egg white lysozyme, proteinase K and thaumatin). Structural analysis performed in the case of hen egg-white lysozyme along with Molecular Dynamics simulations, highlights V 1 's unique behavior, taking advantage of the flexibility of its propanol arm to explore different protein surfaces and form versatile supramolecular interactions.
(© 2024 The Authors. Chemistry - A European Journal published by Wiley-VCH GmbH.)
Databáze: MEDLINE
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