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Crystallizing Membrane Proteins for Structure Determination using Lipidic Mesophases
Published on: November 22, 2010
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Magnesium-aspartate-based crystallization switch inspired from shell molt of crustacean
Jinhui Tao1, Dongming Zhou, Zhisen Zhang
1Department of Chemistry, Center for Biomaterials and Biopathways, Zhejiang University, Hangzhou, Zhejiang 310027, China.
Summary
Magnesium stabilizes amorphous minerals during crustacean molting. Asp-rich proteins then trigger crystallization, revealing a biological switch for shell formation and material fabrication control.
Area of Science:
- Biomineralization
- Materials Science
- Biochemistry
Background:
- Animals like crustaceans molt their exoskeletons cyclically.
- Amorphous calcium mineral phases are stabilized by magnesium during molting.
- Precise regulation of precursor phase transitions in biomineralization remains unclear.
Purpose of the Study:
- To investigate the role of Asp-rich proteins in shell mineralization.
- To understand the mechanism of magnesium-stabilized precursor transition.
- To explore the cooperative effect of magnesium and Asp-rich compounds in biomineralization.
Main Methods:
- In vitro experiments were conducted.
- Studied the effect of magnesium on amorphous calcium carbonate and calcium phosphate stability.
- Investigated the impact of Asp monomer on magnesium-stabilized precursors.
Main Results:
- Magnesium extends the lifetime of amorphous calcium carbonate and calcium phosphate, temporarily inhibiting crystallization.
- Asp-rich proteins reduce the stability of magnesium-stabilized precursors, initiating amorphous-to-crystalline phase transformation.
- An Asp-enhanced magnesium desolvation model explains these kinetic effects.
Conclusions:
- A cooperative effect between magnesium and Asp-rich compounds acts as a crystallization switch in biomineralization.
- This magnesium-Asp-based switch provides a biological model for controlling material fabrication processes.
