Peptides obtained from Partial Hydrolysis of Decalcified Human Dentin Collagen

Abstract

FROM in vitro studies of mineralizing connective tissues, it has been suggested that the arrangement of polarized protein macromolecules in the submicroscopic collagen fibrils may be an important factor in determining whether suitable ‘nucleation centres’ for hydroxyapatite crystals will be present¹. The banded regions of natural and reconstituted collagens are thought to contain relatively high proportions of the bulky basic and acidic amino-acid residues, thus suggesting that the amino-acid residues in collagen are not randomly distributed. This view has already been verified for soft tissue procollagen by an analysis of peptides obtained by enzymatic hydrolysis³. Since soft and hard tissue collagens differ markedly from each other with respect to the availability of their ɛ-amino-groups to dinitrofluorobenzene², as well as in their solubility behaviour¹ and internal molecular structure⁴, it is of interest to compare the composition, amino-acid sequence and structure of highly polar peptides obtained from both types of collagen.