Atomic force microscopy and molecular modeling of protein and peptide binding to calcite.
Oyster shell protein and polyaspartate bound to calcite have been visualized at the atomic and molecular levels by atomic force microscopy. The identities of potential binding sites have been suggested from atomic force microscopy (AFM) images and have been evaluated by molecular modeling. Energies and conformations of binding to (110) and (110) prism faces, (001) basal calcium planes, and (104) cleavage planes are considered. The interaction with the basal plane is strongest and is essentially irreversible. Binding to (110) prism surfaces is also energetically favored and selective for orientations parallel or perpendicular to the c-axis. Binding to (110) faces is significantly weaker and orientation nonspecific. If carboxyl groups of the protein or peptide replace select carbonate ions of the (110) face, the binding energy increases significantly, favoring binding in the parallel direction. Binding to (104) cleavage surfaces is weak and probably reversible. Specific alignment of oyster shell protein molecules on calcite surfaces is shown by AFM, and the relevance to the binding model is discussed.
Department of Chemistry, University of South Alabama, Mobile.
A
A
Wierzbicki
C S
CS
Sikes
J D
JD
Madura
B
B
Drake
D000818:Animals; D001224:Aspartic Acid / Q000032:analysis; D002119:Calcium Carbonate / Q000032:analysis / Q000737:chemistry / Q000378:metabolism*; D005998:Glycine / Q000032:analysis; D008853:Microscopy / Q000379:methods*; D008855:Microscopy, Electron, Scanning; D008958:Models, Molecular; D008970:Molecular Weight; D009678:Nuclear Energy; D010125:Ostreidae; D011485:Protein Binding; D012694:Serine / Q000032:analysis
D001224:Aspartic Acid; D012694:Serine; D002119:Calcium Carbonate; D005998:Glycine