CaCO3 biomineralization: Acidic 8-kDa proteins isolated from aragonitic abalone shell nacre can specifically modify calcite crystal morphology

Abstract

Acidic proteins from many biogenic minerals are implicated in directing the formation of crystal polymorphs and morphologies. We characterize the first extremely acidic proteins purified from biomineralized aragonite. These abalone nacre proteins are two variants of 8.7 and 7.8 kDa designated AP8 (for aragonite proteins of approximately 8 kDa). The AP8 proteins have compositions dominated by Asx (∼35 mol %) and Gly (∼40 mol %) residues, suggesting that their structures have high Ca2+-binding capacity and backbone flexibility. The growth of asymmetrically rounded CaCO3 crystals in the presence of AP8 reveals that both proteins preferentially interact with specific locations on the crystal surface. In contrast, CaCO3 crystals grown with nacre proteins depleted of AP8 retain the morphology of unmodified calcite rhombohedra. Our observations thus identify sites of protein-mineral interaction and provide evidence to support the long-standing theory that acidic proteins are more effective crystal-modulators than other proteins from the same biomineralized material. © 2005 American Chemical Society.