Jump to main content
Jump to site search

Issue 11, 2010
Previous Article Next Article

Mesoscale crystallization of calcium phosphate nanostructures in protein (casein) micelles

Author affiliations

Abstract

Aqueous micelles of the multi-protein calcium phosphate complex, casein, were treated at 60 °C and pH 7 over several months. Although partial dissociation of the micelles into 12 nm sized amorphous calcium phosphate (ACP)/protein nanoparticles occurred within a period of 14 days, crystallization of the ACP nanoclusters into bundles of hydroxyapatite (HAP) nanofilaments was not observed until after 12 weeks. The HAP nanofilaments were formed specifically within the partially disrupted protein micelles suggesting a micelle-mediated pathway of mesoscale crystallization. Similar experiments using ACP-containing synthetic micelles prepared from β-casein protein alone indicated that co-aligned bundles of HAP nanofilaments were produced within the protein micelle interior after 24 hours at temperatures as low as 35 °C. The presence of Mg2+ ions in the casein micelles, as well as a possible synergistic effect associated with the multi-protein nature of the native aggregates, could account for the marked inhibition in mesoscale crystallization observed in the casein micelles compared with the single-component β-casein constructs.

Graphical abstract: Mesoscale crystallization of calcium phosphate nanostructures in protein (casein) micelles

Back to tab navigation

Supplementary files

Publication details

The article was received on 01 Mar 2010, accepted on 13 Apr 2010 and first published on 21 May 2010


Article type: Paper
DOI: 10.1039/C0NR00158A
Citation: Nanoscale, 2010,2, 2400-2405
  •   Request permissions

    Mesoscale crystallization of calcium phosphate nanostructures in protein (casein) micelles

    S. Thachepan, M. Li and S. Mann, Nanoscale, 2010, 2, 2400
    DOI: 10.1039/C0NR00158A

Search articles by author

Spotlight

Advertisements