The nucleation and growth of calcium phosphate crystals at protein and phosphatidylserine liposome surfaces.
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, sigma HAP = 15.0, and with respect to octacalcium phosphate, OCP, sigma OCP = 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.
Nancollas
G H
GH
Department of Chemistry, State University of New York at Buffalo, Amherst, USA.
Tsortos
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A
Zieba
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D002130:Calcium Phosphates / Q000737:chemistry*; D003094:Collagen / Q000737:chemistry; D003460:Crystallization; D005353:Fibronectins / Q000737:chemistry; D008081:Liposomes / Q000737:chemistry; D008855:Microscopy, Electron, Scanning; D008968:Molecular Conformation; D010718:Phosphatidylserines / Q000737:chemistry*
D002130:Calcium Phosphates; D005353:Fibronectins; D008081:Liposomes; D010718:Phosphatidylserines; C485828:alpha-tricalcium phosphate; C485830:tetracalcium phosphate; C485838:calcium phosphate, monobasic, anhydrous; D003094:Collagen; C020243:calcium phosphate; C485829:calcium phosphate, dibasic, anhydrous