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Importance of Electrostatic Interactions Between Calcite Surfaces and Proteins

Published online by Cambridge University Press:  10 February 2011

Aleiandro Rodripuez-Navarro ,
Russell Messier ,
Concepcion Jimenez-Lopez  and
Juan Manuel Garcia-Ruiz
Aleiandro Rodripuez-Navarro
Affiliation:
The PennState Univ, Materials Research Lab, PA, anava@ugr.es
Russell Messier
Affiliation:
The PennState Univ, Materials Research Lab, PA, anava@ugr.es
Concepcion Jimenez-Lopez
Affiliation:
Univ of Granada, IACT-CSIC, Granada, SPAIN
Juan Manuel Garcia-Ruiz
Affiliation:
Univ of Granada, IACT-CSIC, Granada, SPAIN
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Abstract

We have studied the electrostatic interactions of proteins with the calcite surfaces during its subsequent nucleation and growth on a surface. In doing so, a model system of four globular proteins (lysozyme, ribonuclease, myoglobin and α-lactalbumin), having the same size and conformation, but differing in surface properties (i.e. surface charge) was used. Depending on the nature of the charge on the protein, its morphological effect on calcite growth (inhibition of specific crystal faces) varies, with this effect becoming more pronounced as the protein is more negatively charged. To study how the adsorption of proteins affects the growth of calcite along different crystal directions, calcite plates cut with different crystallographic orientations (i.e. (001), (104), (100) and (110)) were used as substrates. The overgrowing calcite crystals show the same orientation as the substrate. The nucleation density also varies with the crystallographic orientation of the calcite substrates, increasing in accordance with the sequence: (110), (100) and (001). Finally, to study how the protein itself controls the orientation of crystals, we used amorphous substrates (glass). After incubation on the glass substrates with negatively charged proteins, an oriented nucleation of the calcite crystals was induced.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 599: Symposium DD – Mineralization in Natural & Synthetic Biomaterials , 1999 , 353
Copyright
Copyright © Materials Research Society 2000

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