We have a collaborative project on proteins that are involved in biomineralization. Some of the accomplishments in this area are given below.

• We have purified two major proteins which contribute significantly to calcium carbonate crystallization and biomineralization in chicken (OC-17) and goose egg shells (ansocalcin). We have completed the amino acid sequences of these proteins. Both proteins are structurally similar to C-type lectin like proteins. Ansocalcin induced the formation of polycrystalline calcite crystal aggregates whereas OC-17 has little influence morphology of calcite crystals. We have designed short peptides based on its structure which mimic parent protein.

• We also purified pelovaterin from turtle eggshells. This protein induces the formation of vaterite crystals. It is a 42-residue protein. Its solution structure shows that it folds similar to β-defensins. This protein also shows some antibacterial activity.

• We showed the formation of transient amorphous calcium carbonate in quail eggshell mineralization.

Key Publications