Effect of Langmuir monolayer of bovine serum albumin protein on the morphology of calcium carbonate

TL;DR

This study investigates how a BSA Langmuir monolayer influences calcium carbonate crystal formation, revealing its role as a template that affects polymorphic phase and morphology, advancing understanding of biomineralization processes.

Contribution

It demonstrates that BSA Langmuir monolayers can control calcium carbonate polymorphs and morphology, providing insights into protein-mediated biomineralization mechanisms.

Findings

BSA monolayer directs calcium carbonate polymorph selection.

Crystal morphology depends on calcium bicarbonate concentration.

BSA influences oriented crystallization and growth patterns.

Abstract

Bovine serum albumin (BSA) Langmuir monolayer, as a model of biomineralization-associated proteins, was used to study its effect on regulated biomineralization of calcium carbonate. The effects of the BSA Langmuir monolayer and the concentration of the subphase solution on the nucleation and growth processes and morphology of the calcium carbonate crystal were investigated. The morphology and polymorphic phase of the resulting calcium carbonate crystals were characterized by scanning electron microscopy (SEM) and X-ray diffraction analysis (XRD). Moreover, the interaction mechanisms of the subphase solution with the BSA Langmuir monolayer were discussed. It was found that BSA Langmuir monolayer could be used as a template to successfully manipulate the polymorphic phase and crystal morphology of calcium carbonate and had obvious influence on the oriented crystallization and growth. The final morphology or aggregation mode of the calcite crystal was closely dependent on the concentration of calcium bicarbonate solution. It is expected that this research would help to better understand the mechanism of biomineralization by revealing the interactions between protein matrices and crystallization of calcium carbonate crystal.