Premium
ESR investigation of the binding of some neutral polyamino acids to synthetic apatite
Author(s) -
Peckauskas R. A.,
Pullman I.,
Termine J. D.
Publication year - 1977
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1977.360160114
Subject(s) - chemistry , macromolecule , apatite , electron paramagnetic resonance , alanine , phosphate , paramagnetism , peptide , mineral , ion , crystallography , nuclear magnetic resonance spectroscopy , inorganic chemistry , stereochemistry , amino acid , nuclear magnetic resonance , organic chemistry , biochemistry , mineralogy , physics , quantum mechanics
Interaction between synthetic crystalline apatitic calcium phosphate and neutral polypeptides [poly( DL ‐alanine), poly( L ‐proline), poly( L ‐hydroxyproline)] was investigated by elecron‐spin‐resonance spectroscopy of mineral‐macromolecule complexes doped with vanadyl ion (VO ++ ) as a paramagnetic probe. Changes in magnetic parameters were interpreted in terms of polypeptide‐induced axial interactions with VO ++ ions that have mineral surface phosphate oxygens as their primary ligands. This implies very close proximity between mineral surface and macromolecular peptide bond dipolar substituents.