Protein Imprinting by Means of Alginate-Based Polymer Microcapsules

Herrero, Edgar P.; Valle, Eva M. Martín del; Peppas, Nicholas A.

doi:10.1021/ie101068z

Cited by 26 publications

(16 citation statements)

References 6 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…There are no natural antibodies specific enough for recognizing these differently sized forms of the hormone. Molecular imprinting is a recent promising technique for the fabrication of biomimetic polymeric recognition sites with a selective affinity for a target molecule (such as a drug, protein or biomacromolecule), which is attracting rapidly increasing interest and many potential applications in the pharmaceutical and biotechnological field [2][3][4][5][6][7][8]. Imprinted materials may constitute an alternative to natural recognition elements.…”

Section: Introductionmentioning

confidence: 99%

“…The method creates materials resembling the binding sites of receptors and antibodies. The polymerization reaction usually occurs by free radical initiation [2][3][4][5][6][7][8][9][10][11][12]. Numerous studies have been conducted to investigate different initiation mechanisms for MIP synthesis, thermal, photo-induced, electrochemical or microwave-assisted methods were employed [7].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Polyacrylamide gels with selective recognition of the tetrameric molecular form of human growth hormone

Kublickas¹,

Werner²,

Voit³

2017

Express Polym. Lett.

View full text Add to dashboard Cite

Abstract. Networks of polyacrylamide were studied for the possibility of imprinting of the oligomeric form of human growth hormone. The tetrameric molecular form of human growth hormone was molecularly imprinted for the first time. The results show that approximately 50-70% (w/w) of the templates (depending on polymerization conditions) could be extracted from the molecularly imprinted acrylamide polymers. The resulting 'gel antibodies' against this form of human growth hormone in the form of granules of polyacrylamide were compared with granules of non-imprinted polymer. The selectivity of the artificial gel antibodies was studied. Investigation of the binding to imprinted polymer of the template hormone, other molecular forms of the hormone and other proteins shows the selectivity of the developed artificial gel antibodies.

show abstract

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Polyacrylamide gels with selective recognition of the tetrameric molecular form of human growth hormone

Kublickas¹,

Werner²,

Voit³

2017

Express Polym. Lett.

View full text Add to dashboard Cite

show abstract

“…[7][8][9][10][11] The highly cross-linked polymers seriously hinder the mass transfer of biological templates and lead to the poor rebinding efficiency. [7][8][9][10][11] The highly cross-linked polymers seriously hinder the mass transfer of biological templates and lead to the poor rebinding efficiency.…”

Section: Introductionmentioning

confidence: 99%

Template size matched film thickness for effectively in situ surface imprinting: a model study of glycoprotein imprints

et al. 2015

RSC Adv.

View full text Add to dashboard Cite

Precisely controlling the material structure is a high requirement for biological target imprinting. In situ surface imprinting immobilized templates can offer thin-film molecular imprints containing site-directed binding sites on substrates, and therefore is appropriate for biological targets. However, the correlation between the required film thickness for superior imprinting effect and the bulk structure of biological template is not clearly understood. Here we use a series of glycoprotein imprinted films as a model to give a semi-quantitative description for their correlation. Glycoproteins with distinguished molecular sizes including ribonuclease B, glucose oxidase and horseradish peroxidase were used as templates.Covalently immobilizing glycoproteins was achieved by using m-aminophenylboronic acid modified SiO 2 or Fe 3 O 4 surface. Dopamine was polymerized onto this surface for glycoprotein imprinting. Varying polymerization time provided a series of thickness tunable imprinting films in nanometer-scale. The binding isotherm study for each glycoprotein imprints with different film thickness was performed. The optimal film thickness for the highest binding capacities and imprinting factors shows a positive correlation with its template size. The each optimized glycoprotein imprints can recognize their template in a simple or complex environment. These results suggest that the thickness of imprinted film should be tailored for matching the geometric size of fixed templates, and reveal the substantial influence of template structure on imprints design.Scheme 1 In situ surface imprinting of immobilized glycoproteins in a film thickness controlled manner. The thickness of imprinted film needs to be tailored for matching individual glycoprotein templates.This journal is

show abstract

“…[19][20][21] The obtained MIPs possessed excellent features including hydrophilicity, non-toxicity, biocompatibility and biodegradation. The natural polymers, like chitosan and alginates, which are water-soluble linear polysaccharides containing plenty of functional groups, are usually chosen as the matrix used to imprint the protein.…”

Section: Introductionmentioning

confidence: 99%

An effective way to imprint protein with the preservation of template structure by using a macromolecule as the functional monomer

Qian

Guan

et al. 2015

RSC Adv.

View full text Add to dashboard Cite

In this study, an assumption that a micromolecular monomer could easily permeate into the inside of a protein and alter its conformation, while an inflexible macromolecular monomer may interact with the surface of the protein and thus maintain the integrity of the template protein's structure was proposed for the first time and confirmed by using circular dichroism and synchronous fluorescence spectroscopy. The protein imprinted hydrogels composed of macromolecular monomers or their equivalent micromolecular monomers were characterized and carried out in the competitive adsorption and adsorption isotherm experiments. The adsorption isotherm behaviours described by the Langmuir model revealed that a higher binding affinity was observed between the template protein and imprinted hydrogels made by a macromolecular monomer. The competitive adsorption results also demonstrated the imprinted hydrogels prepared by the macromolecular monomer exhibited much better specific recognition ability to the template protein. Therefore, the strategy of using a macromolecule to imprint could effectively overcome the mutability of protein during the preparation of imprinted polymers, and consequently would promote the development of imprinting technology.Scheme 1 The influence of macromolecular chain and micromolecular monomer on the conformation of template protein.

show abstract

Protein Imprinting by Means of Alginate-Based Polymer Microcapsules

Cited by 26 publications

References 6 publications

Polyacrylamide gels with selective recognition of the tetrameric molecular form of human growth hormone

Polyacrylamide gels with selective recognition of the tetrameric molecular form of human growth hormone

Template size matched film thickness for effectively in situ surface imprinting: a model study of glycoprotein imprints

An effective way to imprint protein with the preservation of template structure by using a macromolecule as the functional monomer

Contact Info

Product

Resources

About