Aerosol-generated sol-gel-derived thin films as biosensing platforms

Jordan, Jeffrey M.; Dunbar, Richard A.; Bright, Frank V.

doi:10.1016/0003-2670(96)00154-7

Cited by 68 publications

(59 citation statements)

References 27 publications

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“…These antibodies are then able to recognize specifically the target analyte (hapten) and can be used as immunosensors for the detection of traces of chemical species. Sol-gel encapsulated antibodies have been used for the detection of various chemicals such as fluorescein [67,68], dinitrobenzene (DNB) [69], dinitrophenyl (DNP) [70]. The high binding constants of antibodies to antigens make them ideal for chromatographic separation.…”

Section: Antibody-based Affinity Biosensorsmentioning

confidence: 99%

Bioactive Sol‐Gel Hybrids

Livage¹,

Coradin²,

Roux³

2003

Functional Hybrid Materials

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Section: Antibody-based Affinity Biosensorsmentioning

confidence: 99%

Bioactive Sol‐Gel Hybrids

Livage¹,

Coradin²,

Roux³

2003

Functional Hybrid Materials

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“…An emerging method for immobilization of proteins is their entrapment into a porous, inorganic silicate matrix that is formed via a low-temperature sol-gel processing method. 10,11 Numerous reports have described both fundamental aspects of entrapped proteins, such as their conformation, 12-14 dynamics, 15-17 accessibility, 14 and stability, [31][32][33][34][35][36][37][38] and their many applications for catalysis, sensing, and affinity chromatography. 11 However, few reports describe the entrapment of kinases into sol-gel derived silica, 39 and no reports describe studies of entrapped protein tyrosine kinases.…”

mentioning

confidence: 99%

Entrapment of Src Protein Tyrosine Kinase in Sugar-Modified Silica

et al. 2004

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A novel sugar-modified silica has been used to entrap for the first time a protein tyrosine kinase (PTK). Silane precursors bearing covalently attached gluconamide moieties were used in combination with the biocompatible precursor diglycerylsilane (DGS) to generate sol-gel derived silica that was able to encapsulate highly active Src PTK and preserve the activity of the enzyme over multiple uses. The relative activity of the enzyme was assayed using a LANCE based fluorescence resonance energy transfer method involving time-gated detection of fluorescence from a europium labeled antiphosphotyrosine antibody and Cy5 labeled streptavidin upon mutual binding to biotinylated phosphopeptides. Using this detection method, with the antibody and streptavidin external to the sol-gel matrix, it was possible to detect the phosphorylation of peptides with molecular weights of up to 2300 Da using the entrapped enzyme in N-(3-triethoxysilylpropyl)gluconamide (GLTES) doped glasses. Src kinase-doped glasses, derived from precursors such as tetramethyl orthosilicate, tetraethyl orthosilicate, or DGS that did not contain GLTES, provided no detectable enzyme activity. The addition of 1 mM ATP to the GLTES/DGS sol before the encapsulation of the protein increased the activity of the enzyme in the resulting gel, likely through a ligand-based stabilization mechanism. The use of such a system for determination of PTK activity and inhibition is demonstrated, setting the stage for the development of chromatographic and microarray based methods for the screening of kinase inhibitors.

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“…73 Indeed, this route increased gelation times to the range of 5e15 min and permitted spray coating of lab-scale structured packing. The optimized formulation developed as described in the previous sections using spherical random packing exhibited very fast gelation times, on the order of 15e30 s, amenable to stir coating but not dip or spray coating.…”

Section: Coatings On Structured Packingmentioning

confidence: 99%