Asprich peptides are occluded in calcite and permanently disorder biomineral crystals.
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 (CaCO(3)) 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.
Metzler
Rebecca A
RA
Department of Physics, University of Wisconsin-Madison, 1150 University Avenue, Madison, Wisconsin 53706, USA.
Tribello
Gareth A
GA
Parrinello
Michele
M
Gilbert
P U P A
PU
D040761:Biomimetic Materials / Q000737:chemistry*; D002119:Calcium Carbonate / Q000737:chemistry*; D008968:Molecular Conformation; D010446:Peptide Fragments / Q000737:chemistry*; D056928:X-Ray Absorption Spectroscopy
D010446:Peptide Fragments; D002119:Calcium Carbonate