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Issue 1, 2019
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Avidin-adsorbed peptide–calcium phosphate composites exhibiting high biotin-binding activity

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Techniques harnessing the strong interactions of the avidin–biotin system are frequently used in biosensing and protein separation. Hydroxyapatite (Ca10(PO4)6(OH)2, HAp) is a calcium phosphate compound known to have a strong affinity for various proteins. In this study, the adsorption ability of avidin on composites and its binding activity to biotin were investigated using two types of poly(L-glutamic acid)-containing calcium phosphate composites (pGlu-HAp). The morphologies of pGlu-HAp including poly(α-glutamic acid) and poly(γ-glutamic acid) showed plate-like and sheet-like particles, respectively, due to the effects of the peptide structure. Furthermore, these particles exhibited the high adsorption capacity of avidin; the maximum adsorption amounts for poly(α-glutamic acid)-HAp and poly(γ-glutamic acid)-HAp were 776 and 302 μg mg−1 HAp, respectively. In addition, the equilibrium data for the adsorption of avidin on two pGlu-HAp-fitted Langmuir isotherm models correspond to a monolayer. The difference in the amount of adsorbed avidin on the two pGlu-HAp composites was influenced by the density of the carboxyl groups in pGlu-HAp. This revealed that avidin adsorbed on pGlu-HAp was able to bind four biotin molecules, and biotinylated protein was separated from protein mixtures by avidin-adsorbed pGlu-HAp. These results indicate that these particles would be appropriate in the development of biosensing and bioseparation tools.

Graphical abstract: Avidin-adsorbed peptide–calcium phosphate composites exhibiting high biotin-binding activity

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Publication details

The article was received on 04 Oct 2018, accepted on 17 Nov 2018 and first published on 19 Nov 2018

Article type: Paper
DOI: 10.1039/C8NJ05024D
New J. Chem., 2019,43, 427-435

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    Avidin-adsorbed peptide–calcium phosphate composites exhibiting high biotin-binding activity

    S. Kojima, F. Nagata, M. Inagaki, S. Kugimiya and K. Kato, New J. Chem., 2019, 43, 427
    DOI: 10.1039/C8NJ05024D

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