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Electrically polarized biphasic calcium phosphates: adsorption and release of bovine serum albumin.


ABSTRACT: In this study, we applied electrical polarization technique to increase adsorption and control protein release from biphasic calcium phosphate (BCP). Three different biphasic calcium phosphate (BCP) composites, with hydroxyapatite (HAp) and ?-tricalcium phosphate (?-TCP), were processed and electrically polarized. Our study showed that stored charge was increased in the composites with the increase in HAp percentage. Adsorption of bovine serum albumin (BSA), as a model protein, on the poled as well as unpoled surfaces of the composites was studied. The highest amount of BSA adsorption was obtained on positively poled surfaces of each composite. Adsorption isotherm study suggested a multilayer adsorption of BSA on the BCP composites. The effect of electrical polarization on BSA release kinetics from positively charged BCP surfaces was studied. A gradual increase in percent BSA release from positively charged BCP surfaces with decreasing stored charge was observed. Our study showed that the BCP based composites have the potential to be used as a drug or growth factor delivery vehicle.

SUBMITTER: Tarafder S 

PROVIDER: S-EPMC2979312 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature

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Electrically polarized biphasic calcium phosphates: adsorption and release of bovine serum albumin.

Tarafder Solaiman S   Banerjee Shashwat S   Bandyopadhyay Amit A   Bose Susmita S  

Langmuir : the ACS journal of surfaces and colloids 20101012 22


In this study, we applied electrical polarization technique to increase adsorption and control protein release from biphasic calcium phosphate (BCP). Three different biphasic calcium phosphate (BCP) composites, with hydroxyapatite (HAp) and β-tricalcium phosphate (β-TCP), were processed and electrically polarized. Our study showed that stored charge was increased in the composites with the increase in HAp percentage. Adsorption of bovine serum albumin (BSA), as a model protein, on the poled as w  ...[more]

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