Asprich Peptides Are Occluded in Calcite and Permanently Disorder Biomineral Crystals

Rebecca A. Metzler, Gareth A. Tribello, Michele Parrinello, P. U. P. A. Gilbert

Research output: Contribution to journalArticle

55 Citations (Scopus)

Abstract

Macromolecules are a minority but important component of the minerals formed by living organisms, or biominerals. The role these macromolecules play at the early stages of biomineral formation, as well as their long-term and long-range effects on the mature biomineral, is poorly understood. A 42-amino acid peptide, asp2, was derived from the Asprich family of proteins. In this study we present X-ray absorption near-edge structure spectroscopy and X-ray photoelectron emission microscopy data from the asp2 peptide, the calcite (CaCO3) crystals, and the peptide + crystal composites. The results clearly show that asp2 is occluded in fully formed biomineral crystals and slightly but permanently disorders the crystal structure at short- and long-range distances.

Original languageEnglish
Pages (from-to)11585-11591
Number of pages7
JournalJournal of the American Chemical Society
Volume132
Issue number33
DOIs
Publication statusPublished - 25 Aug 2010

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