Adsorption of Bovine Serum Albumin and Lysozyme on Hydrophobic Calcium Hydroxyapatites

Kandori, Kazuhiko; Mukai, Megumi; Fujiwara, Aya; Yasukawa, Akemi; Ishikawa, Tatsuo

doi:10.1006/jcis.1998.6060

Cited by 39 publications

(32 citation statements)

References 15 publications

(17 reference statements)

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“…There are other publications that investigate the adsorption of proteins on calcium phosphates using zeta potential and UV/Vis spectroscopy measurements as characterization methods. [18,[28][29][30][31][32][33][34][35][36][37][38] However, the investigations are not systematic and in most cases only the zeta potential of the powder was measured without determining the amount of adsorbed protein. The development of the zeta potential as a function of protein addition was not analysed.…”

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Bovine Serum Albumin and Lysozyme Adsorption on Calcium Phosphate Particles

2010

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Two model proteins that are oppositely charged at neutral pH – bovine serum albumin (BSA) and lysozyme, with acidic and alkaline isoelectric points, respectively – are used to investigate the protein adsorption behaviour of hydroxyapatite and beta‐tricalcium phosphate (β‐TCP) particles. Both calcium phosphate based particles are highly relevant for the fabrication of bioactive and resorbable bone implants. The investigations are carried out by combining zeta potential and Vis spectroscopy measurements. The changes of zeta potential and isoelectric point are determined as a function of added protein. Both proteins form a monolayer on β‐TCP, while on hydroxyapatite only semi‐monolayers were measured. For BSA, a side‐on adsorption mode is suggested, whereas end‐on adsorption appears to be most likely for lysozyme. The zeta potential curves as a function of adsorbed protein show that plateaus of the protein amounts adsorbed increase with charge saturation. In addition, the spatial charge distribution of both proteins is modelled to get a further understanding of the initial adsorption orientation of the biomolecules, supporting the findings from the experimental data. The reported findings can be transferred to the adsorption behaviour of a variety of proteins on calcium phosphate surfaces and are helpful for the fabrication of bone‐analogous calcium phosphate/protein nanocomposites.

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Bovine Serum Albumin and Lysozyme Adsorption on Calcium Phosphate Particles

2010

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“…BSA is a globular ellipsoid (14 × 4 × 4 nm), with a molecular mass of approximately 69 kDa, and an isoelectric point of 4.7 (Kandori et al, 1999).…”

Section: Methodsmentioning

confidence: 99%

The effects of ligand chain length, salt concentration and temperature on the adsorption of bovine serum albumin onto polypropyleneglycol–Sepharose

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Phillips

et al. 2005

Biomedical Chromatography

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The interaction thermodynamics associated with bovine serum albumin adsorption on polypropylene glycol (n=3)-Sepharose CL-6B and polypropylene glycol (n=7)-Sepharose CL-6B, using ammonium sulfate as the modulator was studied. Analysis of data under linear conditions was accomplished with the stoichiometric displacement retention model, preferential interaction approach and van't Hoff plots applied to HIC systems. Preferential interaction analysis indicated a strong entropic driving force under linear conditions, due to the release of a large amount of solvent on adsorption. In contrast, flow microcalorimetry under overloaded conditions showed that the adsorption of bovine serum albumin may be entropically or enthalpically driven. It is postulated that adsorption in the nonlinear region is influenced by the degree of water release, protein-protein interactions on the surface, reorientation of ligand, and conformational changes in the protein.

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“…The C site, the Ca 2+ ion-rich surface, has a high affinity to the negatively charged molecules. On the other hand, the P sites, the PO 3À 4 and OH À ion-rich surface, have a high affinity to the positively charged molecules [16]. This surface electric property of HAp is valuable for separating and isolating multiple molecules to use them as packing materials for the column chromatography [17,18].…”

Section: Introductionmentioning

confidence: 99%