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Ionic-liquid-functionalized mineral particles for protein crystallization

DOI: 10.1021/acs.cgd.5b00403 DOI Help

Authors: M. Kowacz (Universidade Nova de Lisboa) , M. Marchel (Universidade Nova de Lisboa) , Lina Juknaite (Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa) , Jose Esperanca (Instituto de Tecnologia Química e Biológica) , M. J. Romão (Universidade Nova de Lisboa) , A. L. Carvalho (Universidade Nova de Lisboa) , Luis Paulo Rebelo (Instituto de Tecnologia Química e Biológica)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Crystal Growth & Design , VOL 15 , PAGES 2994 - 3003

State: Published (Approved)
Published: June 2015
Diamond Proposal Number(s): 8425

Abstract: Nucleation is a critical step determining the outcome of the entire crystallization process. Finding an effective nucleant for protein crystallization is of utmost importance for structural biology. The latter relies on good-quality crystals to solve the three-dimensional structures of macromolecules. In this study we show that crystalline barium sulfate (BaSO4) with an etched and/or ionic liquid (IL)-functionalized surface (1) can induce protein nucleation at concentrations well below the concentration needed to promote crystal growth under control conditions, (2) can shorten the nucleation time, (3) can increase the growth rate, and finally (4) may help to improve the protein crystal morphology. These effects were shown for lysozyme, RNase A, trypsin, proteinase K, myoglobin, and hemoglobin. Therefore, the use of BaSO4 particles enables us to reduce the amount of protein in crystallization trials and increases the chance of obtaining protein crystals of the desired quality. In the context of the underlying mechanism, it is shown that the protein–solid contact formation is governed by the interaction of the polar compartments of the biomacromolecule with the support. The tendency of a protein to concentrate near the solid surface is enhanced by both the hydrophobicity of the protein and that of the surface (tuned by the functionalizing IL). These mechanisms of interaction of biomacromolecules with inorganic hydrophilic solids correspond to the principles of amphiphilic IL–mineral interactions.

Journal Keywords: Crystallization; Crystals; Nanoparticles; Nucleation; Peptides and proteins

Subject Areas: Chemistry, Biology and Bio-materials

Instruments: I02-Macromolecular Crystallography

Other Facilities: ID29 at ESRF

Added On: 12/01/2016 13:09

Discipline Tags:

Biochemistry Chemistry Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)