Biomimetic mineralization with enhanced hydrogen-bond interactions for protein stabilization

Area of Science:

• Biomaterials Science
• Protein Engineering
• Biomineralization

Background:

• Proteins are valuable for industrial and therapeutic applications but are limited by heat sensitivity.
• Existing biomineralization strategies struggle to adequately protect proteins from thermal degradation.

Purpose of the Study:

• To develop a biomimetic mineralization strategy for creating condensed protein-calcium phosphate hybrids.
• To enhance the thermostability and preservation of proteins using this novel hybrid structure.

Main Methods:

• A biomimetic nanocluster of calcium phosphate capped with triethylamine was used as a mineral ion precursor.
• This precursor facilitated the integration of higher protein concentrations into a homogeneous condensed structure.
• Spectroscopic analysis confirmed enhanced hydrogen bond interactions between protein and mineral components.

Main Results:

• The protein-calcium phosphate hybrid demonstrated significantly improved thermostability.
• Lysozyme and catalase retained over 75% activity after heating to 120 °C.
• The novel hybrid outperformed conventional biomineralization for long-term protein preservation.

Conclusions:

• The developed biomimetic platform offers an effective strategy for protein preservation and enhancement of thermostability.
• This research provides new insights into protein-mineral interactions, enabling better future control and modification of proteins.