Functional peptides play an important role in the formation of biominerals. Here we focus on peptides involved in mineralization of the exoskeleton of a crayfish. New recombinant peptides are designed and synthesized on the basis of an acidic functional peptide, CAP-1, derived from the exoskeleton of a crayfish. We have examined the effect of these peptides on the hybrid formation of calcium carbonate and organic molecules in aqueous solution. In the presence of these recombinant peptides having chitin binding moieties, platelike tripodal calcite crystals are formed on the chitin matrix with unidirectional crystallographic orientation. Two kinds of interactions, (1) interactions between an acidic part of the peptides and calcium ions and (2) specific binding interactions of the peptides to chitin, are essential for the formation of the oriented crystals and the induction of specific morphologies. Moreover, the sizes of crystallites decrease with increasing the number of acidic parts of mutational peptides. The bioinspired design of peptides that control the interface of inorganic and organic domains may pave the way for an opportunity to build new hybrid structures.
ASJC Scopus subject areas
- Physical and Theoretical Chemistry