The Nucleation and Growth of Calcium Phosphate Crystals at Protein and Phosphatidylserine Liposome Surfaces

Authors

G. H. Nancollas, State University of New York at Buffalo
A. Tsortos, State University of New York at Buffalo
A. Zieba, State University of New York at Buffalo

Abstract

The kinetics of calcium phosphate crystal growth at the surfaces of proteins and phospholipids has been investigated using free drift and constant composition methods in supersaturated calcium phosphate solutions (relative supersaturations: with respect to hydroxyapatite, HAP, σHAP = 15.0, and with respect to octacalcium phosphate, OCP, σOCP = 1. 9). Fibrinogen and collagen molecules adsorbed at hydrophobic surfaces as well as uncross-linked collagen fibrils induce ion binding and subsequent nucleation of calcium phosphate. The formation of OCP on phosphatidylserine vesicles introduced to highly supersaturated calcium phosphate solutions probably involves the interaction of the calcium ions with the ionized carboxylic groups of the phospholipid.

Recommended Citation

Nancollas, G. H.; Tsortos, A.; and Zieba, A. (1996) "The Nucleation and Growth of Calcium Phosphate Crystals at Protein and Phosphatidylserine Liposome Surfaces," Scanning Microscopy: Vol. 10: No. 2, Article 17.
Available at: https://digitalcommons.usu.edu/microscopy/vol10/iss2/17