Protein Self-Assembly States Modulate Lithium Carbonate Biomineralization: From Ion Chelation to Nucleation Sites
Year: 2025
Type: article
Abstract: High Resolution Image Download MS PowerPoint Slide Understanding protein–salt interactions is important for controlling crystallization, including biomineralization, biopharmaceutical purification, biocatalytic enzymes, and environmental biointerfaces. This study for the first time investigated interactions between three proteins (lysozyme, red fluorescence protein, and bovine hemoglobin) and Li 2 CO 3 (formation from the reaction of LiCl with Na 2 CO 3 ) under different protein and salt concentrations. For the crystallization of Li 2 CO 3, at low supersaturation ( S ), the proteins inhibited Li 2 CO 3 nucleation by 20–40% through chelation. At high S, the proteins accelerated nucleation by 10–40%. The dual effects of the protein on Li 2 CO 3 biomineralization have been discussed. With the increase S of Li 2 CO 3, the dispersion state of proteins in solution undergoes a transition from dimers to oligomers and finally to aggregates. In all ranges of S, the protein reduced the agglomeration of Li 2 CO 3 crystals. In lysozyme crystallization, increasing the Li 2 CO 3 concentration yielded a larger number of smaller crystals. At equal concentration of lysozyme, twice more of LiCl and Na 2 CO 3 in the solution led to more than 5 times the crystal number and 5 times smaller average crystal size. The interactions among protein molecules, salt ions in solution, and Li 2 CO 3 crystals have been discussed. Dynamic light scattering measurements and the fluorescence microscopy image suggest that the dual effect of proteins on Li 2 CO 3 crystallization at different supersaturation levels is associated with protein molecular aggregation under varying salt concentrations, resulting in both thermodynamic and kinetic influences on the crystallization process.
Source: Biomacromolecules
Authors: Zhichun Lin, Yizhen Yan, Archie Hunter, Huaiyu Yang
Institution: Loughborough University
Language: English
Subfield: Materials Chemistry
Field: Materials Science
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $4,500
Funder: Loughborough University
OpenAlex ID: W4417288940