Use of silane monomers for molecular imprinting and enzyme entrapment in polysiloxane-coated porous silica

Glad, Magnus; Norrlöw, Olof; Sellergren, Börje; Siegbahn, Nils; Mosbach, Klaus

doi:10.1016/s0021-9673(01)95465-2

Cited by 233 publications

(101 citation statements)

References 18 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Sol-Gel Imprinting-The first reported successful protein imprint was by the group of Mosbach (62). They developed a method of coating an imprinted polymer for the glycoprotein transferrin (Tf) onto the surface of porous silica beads.…”

Section: Dmentioning

confidence: 99%

See 1 more Smart Citation

From 3D to 2D: A Review of the Molecular Imprinting of Proteins

Turner¹,

Jeans²,

Brain³

et al. 2006

Biotechnol. Prog.

186

217

View full text Add to dashboard Cite

Molecular imprinting is a generic technology that allows for the introduction of sites of specific molecular affinity into otherwise homogeneous polymeric matrices. Commonly this technique has been shown to be effective when targeting small molecules of molecular weight <1500, while extending the technique to larger molecules such as proteins has proven difficult. A number of key inherent problems in protein imprinting have been identified, including permanent entrapment, poor mass transfer, denaturation, and heterogeneity in binding pocket affinity, which have been addressed using a variety of approaches. This review focuses on protein imprinting in its various forms, ranging from conventional bulk techniques to novel thin film and monolayer surface imprinting approaches.

show abstract

Section: Dmentioning

confidence: 99%

“…Further examples of each technique are required, using a wider range of proteins. The potential demonstrated with sol-gels is high (93), but as yet only three protocols have been reported (60,62,75).…”

Section: Conclusion and Future Outlookmentioning

confidence: 99%

From 3D to 2D: A Review of the Molecular Imprinting of Proteins

Turner¹,

Jeans²,

Brain³

et al. 2006

Biotechnol. Prog.

186

217

View full text Add to dashboard Cite

show abstract

“…[5][6][7][8][9][10]). Comparatively few reports describe imprinting inorganic materials [11][12][13][14][15][16].…”

Section: Introductionmentioning

confidence: 99%

Protein-imprinted polysiloxane scaffolds

2007

View full text Add to dashboard Cite

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 0.3μg m −2 for low loading of RNase to 152μg m −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 14 kD). 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.

show abstract

“…The concentration in human serum is around 30 µM (Welch, 1992). The first molecularly imprinted polymer (MIP) for Trf was presented by the Mosbach group in 1985: they imprinted a polymer on porous silica support that addressed surface exposed glycans of the target Trf (Glad et al, 1985). Following this route, Liu's group introduced UV-initiated photolithographic molecular imprinting based on boronate affinity as a general approach for the imprinting of glycoproteins (L. .…”

Section: Introductionmentioning

confidence: 99%

Electrosynthesized MIPs for transferrin: Plastibodies or nano-filters?

Zhang

Yarman

Erdőssy

et al. 2018

Biosensors and Bioelectronics

View full text Add to dashboard Cite

Molecularly imprinted polymer (MIP) nanofilms for transferrin (Trf) have been synthesized on gold surfaces by electro-polymerizing the functional monomer scopoletin in the presence of the protein target or around pre-adsorbed Trf. As determined by atomic force microscopy (AFM) the film thickness was comparable with the molecular dimension of the target. The target (re)binding properties of the electro-synthesized MIP films was evaluated by cyclic voltammetry (CV) and square wave voltammetry (SWV) through the target-binding induced permeability changes of the MIP nanofilms to the ferricyanide redox marker, as well as by surface plasmon resonance (SPR) and surface enhanced infrared absorption spectroscopy (SEIRAS) of the immobilized protein molecules. For Trf a linear concentration dependence in the lower micromolar range and an imprinting factor of ~5 was obtained by 2 SWV and SPR. Furthermore, non-target proteins including the iron-free apo-Trf were discriminated by pronounced size and shape specificity. Whilst it is generally assumed that the rebinding of the target or of cross-reacting proteins exclusively takes place at the polymer here we considered also the interaction of the protein molecules with the underlying gold transducers. We demonstrate by SWV that adsorption of proteins suppresses the signal of the redox marker even at the bare gold surface and by SEIRAS that the treatment of the MIP with proteinase K or NaOH only partially removes the target protein. Therefore, we conclude that when interpreting binding of proteins to directly MIP-covered gold electrodes the interactions between the protein and the gold surface should also be considered.

show abstract

Use of silane monomers for molecular imprinting and enzyme entrapment in polysiloxane-coated porous silica

Cited by 233 publications

References 18 publications

From 3D to 2D: A Review of the Molecular Imprinting of Proteins

From 3D to 2D: A Review of the Molecular Imprinting of Proteins

Protein-imprinted polysiloxane scaffolds

Electrosynthesized MIPs for transferrin: Plastibodies or nano-filters?

Contact Info

Product

Resources

About