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 28 mg BSA protein for 24 h.•BSA loaded HA releases 75 wt% BSA in the period of 96 h.

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 (28 mg BSA/gm of nanorod HA) of BSA within 48 h in comparison with counterpart fibroid and spherical morphologies. Slow and steady BSA release (75 wt% of adsorbed BSA in 96 h) from nanorod HA is found as futuristic drug delivery media.

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