Human insulin polymorphism upon ligand binding and pH variation: the case of 4-ethylresorcinol

This study focuses on the effects of the organic ligand 4-ethylresorcinol on the crystal structure of human insulin using powder X-ray crystallography. For this purpose, systematic crystallization experiments have been conducted in the presence of the organic ligand and zinc ions within the pH range...

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Bibliographic Details
Published in:IUCrJ 2015-09, Vol.2 (Pt 5), p.534-544
Main Authors: Fili, S, Valmas, A, Norrman, M, Schluckebier, G, Beckers, D, Degen, T, Wright, J, Fitch, A, Gozzo, F, Giannopoulou, A E, Karavassili, F, Margiolaki, I
Format: Article
Language:English
Subjects:
4-ethylresorcinol
Chemical Sciences
Crystal structure
Crystallization
diabetes
Diffraction
Genetic aspects
Genetic polymorphisms
human insulin
Identification and classification
Insulin
Ligands
Ligands (Biochemistry)
pH variation
Physiological aspects
powder diffraction
Protein binding
Research Papers
synchrotron radiation
X-ray diffraction
X-rays
Zinc
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Summary:This study focuses on the effects of the organic ligand 4-ethylresorcinol on the crystal structure of human insulin using powder X-ray crystallography. For this purpose, systematic crystallization experiments have been conducted in the presence of the organic ligand and zinc ions within the pH range 4.50-8.20, while observing crystallization behaviour around the isoelectric point of insulin. High-throughput crystal screening was performed using a laboratory X-ray diffraction system. The most representative samples were selected for synchrotron X-ray diffraction measurements, which took place at the European Synchrotron Radiation Facility (ESRF) and the Swiss Light Source (SLS). Four different crystalline polymorphs have been identified. Among these, two new phases with monoclinic symmetry have been found, which are targets for the future development of microcrystalline insulin drugs.
ISSN:2052-2525
2052-2525
DOI:10.1107/S2052252515013159