Study of BSA protein adsorption/release on hydroxyapatite nanoparticles

•Morphology, Ca:P and crystallinity have influence on protein adsorption.•BSA adsorption on HA nanoparticle follows Langmuir isotherm.•BSA protein secondary structure remains unchanged for BSA–HA conjugates.•One gram HA nanorod adsorbs 28mg BSA protein for 24h.•BSA loaded HA releases 75wt% BSA in th...

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Veröffentlicht in:Applied surface science 2013-12, Vol.286, p.99-103
Hauptverfasser: Swain, Sanjaya Kumar, Sarkar, Debasish
Format: Artikel
Sprache:eng
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Zusammenfassung:•Morphology, Ca:P and crystallinity have influence on protein adsorption.•BSA adsorption on HA nanoparticle follows Langmuir isotherm.•BSA protein secondary structure remains unchanged for BSA–HA conjugates.•One gram HA nanorod adsorbs 28mg BSA protein for 24h.•BSA loaded HA releases 75wt% BSA in the period of 96h. Three different spherical, rod and fibrous morphologies of hydroxyapatite (HA) nanoparticles have been prepared through control over the processing parameters like temperature, pH and Ca:P ratio. Protein adsorption/release with respect to HA nanoparticle morphologies are investigated using model protein bovine serum albumin (BSA). BSA adsorption on HA nanoparticles follows Langmuir adsorption isotherm. Thermal analysis and FT-IR spectrum confirms the BSA adhesion and retention of their secondary structure. High surface area with high Ca:P ratio nanorod adsorbs relatively more amount (28mg BSA/gm of nanorod HA) of BSA within 48h in comparison with counterpart fibroid and spherical morphologies. Slow and steady BSA release (75wt% of adsorbed BSA in 96h) from nanorod HA is found as futuristic drug delivery media.
ISSN:0169-4332
1873-5584
DOI:10.1016/j.apsusc.2013.09.027