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

Author:

Roux Amandine12ORCID,Alsalman Zaynab3ORCID,Jiang Tao1,Mulatier Jean‐Christophe1,Pitrat Delphine1,Dumont Elise45ORCID,Riobé François16ORCID,Gillet Natacha1ORCID,Girard Eric3ORCID,Maury Olivier1ORCID

Affiliation:

1. Univ. Lyon École Normale Supérieure de Lyon CNRS UMR 5182 Laboratoire de Chimie 46 allée d'Italie 69007 Lyon France

2. Polyvalan SAS Lyon France

3. Univ Grenoble Alpes CEA, CNRS, IBS F-38000 Grenoble France

4. Univ. Côte d'Azur CNRS Institut de Chimie de Nice UMR 7272 06108 Nice France

5. Institut Universitaire de France 5 rue Descartes 75005 Paris France

6. Univ Bordeaux Bordeaux INP CNRS Institut de Chimie de la Matière Condensée de Bordeaux 33608 Pessac France

Abstract

AbstractCrystallophores 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 G1. In particular, the V1 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 V1′s unique behavior, taking advantage of the flexibility of its propanol arm to explore different protein surfaces and form versatile supramolecular interactions.

Funder

Agence Nationale de la Recherche

Région Auvergne-Rhône-Alpes

Bpifrance

Publisher

Wiley

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