Protein-imprinted polysiloxane scaffolds.

Abstract:

:Molecular imprinting is a technique used to create specific recognition sites on the surface of materials. Although widely developed for chromatographic separation of small molecules, this approach has not been adequately investigated for biomaterial applications. Thus, the objective of these experiments was to explore the potential of molecular imprinting for creating biomaterials that preferentially bind specific proteins. Macroporous polysiloxane (silica) scaffolds were imprinted with either lysozyme or RNase A using sol-gel processing. The quantity of surface-accessible protein, which was related to the number of potential binding sites, was varied by changing the amount of protein loaded into the sol. Up to 62% of loaded protein was accessible. The amount of protein per unit surface area ranged from 0.3microgm(-2) for low loading of RNase to 152microgm(-2) for high loading of lysozyme. Protein-imprinted scaffolds were then evaluated for their ability to preferentially recognize the template biomolecule when incubated in mixtures containing both the imprinted protein and a competitor protein of comparable size (approximately 14kD). In solutions containing a single protein, up to 3.6 times more template bound compared with the competitor. Furthermore, in solutions containing equal amounts of both molecules, the porous scaffolds bound up to three times more template than the competitor protein, which is a level of preferential binding similar to values reported in the molecular imprinting literature for both organic and inorganic materials.

journal_name

Acta Biomater

journal_title

Acta biomaterialia

authors

Lee K,Itharaju RR,Puleo DA

doi

10.1016/j.actbio.2007.01.003

subject

Has Abstract

pub_date

2007-07-01 00:00:00

pages

515-22

issue

4

eissn

1742-7061

issn

1878-7568

pii

S1742-7061(07)00017-7

journal_volume

3

pub_type

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