Abstract
Short-peptide supramolecular (SPS) hydrogels are a class of materials that have been found to be useful for (bio)technological applications thanks to their biocompatible nature. Among the advantages reported for these peptides, their economic affordability and easy functionalization or modulation have turned them into excellent candidates for the development of functional biomaterials. We have recently demonstrated that SPS hydrogels can be used to produce high-quality protein crystals, improve their properties, or incorporate relevant materials within the crystals. In this work, we prove that hydrogels based on methionine and tyrosine are also good candidates for growing high-quality crystals of the three model proteins: lysozyme, glucose isomerase, and thaumatin.
Highlights
In the biological macromolecules field, where sample impurity has been a relevant issue for many years, it is generally thought that the participation of any new additive, such as gel precursors, could be detrimental to the crystallization, affecting the final crystal properties
We have shown in this work that two new Short-peptide supramolecular (SPS) hydrogels based on methionine and tyrosine are suitable for the crystallization of proteins, namely lysozyme, thaumatin, and glucose isomerase
The obtained crystals diffracted X-rays at the maximum expected limit, demonstrating, once more, the benefits of growing crystals in media with mass transport controlled by diffusion
Summary
In the biological macromolecules field, where sample impurity has been a relevant issue for many years, it is generally thought that the participation of any new additive, such as gel precursors, could be detrimental to the crystallization, affecting the final crystal properties. It is well accepted that the use of gels may help control and facilitate the growth of bigger and higher-quality crystals for inorganic materials [1,2,3]. The use of gels is still largely unexplored in applications for protein crystallography [5]. Already in 1999, the term reinforced protein crystal was introduced for crystals grown in silica gels, which showed a higher robustness due to the incorporation of the gel fibers into the crystalline network [6]. It was demonstrated that protein crystals grown in agarose are more stable against osmotic shocks generated when a crystal is transferred from its mother liquid to a solution containing for example a ligand, inhibitor, cryoprotectant agent, or heavy atom [7,8]. Gels facilitate handling crystals [9], avoiding their deterioration, and making it even the collection of diffraction data at room temperature possible [6,10]
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