2008
DOI: 10.1039/b810248a
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Surface molecularly imprinted nanowire for protein specific recognition

Abstract: A surface molecularly imprinted nanowire is designed by chemical polymerization of dopamine in neutral aqueous solution, which shows high binding capacity and acceptable specific recognition behavior towards template proteins.

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Cited by 145 publications
(97 citation statements)
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“…Although MIPs have been successfully developed against a wide range of small molecules, the imprinting of macromolecules like protein has proven to be more difficult. The major problems are entrapment of macromolecular templates in polymers, unfavorable kinetics of the adsorption and desorption process, the production of heterogeneous sites and the sensitivity of biomacromolecule to denaturation (Bereli et al, 2008;Ouyang et al, 2008;Jin and Tang, 2009;Flavin and Resmini, 2009). To resolve these problems, surface polymerization has been proposed to prepare the MIPs film on a solid support substrate, which can improve mass transfer and reduce permanent entrapment of the template, but these methods also reduce the number of imprinting sites (Boninia et al, 2007;Wang et al, 2009a,b;Zhai et al, 2009).…”
Section: Introductionmentioning
confidence: 97%
“…Although MIPs have been successfully developed against a wide range of small molecules, the imprinting of macromolecules like protein has proven to be more difficult. The major problems are entrapment of macromolecular templates in polymers, unfavorable kinetics of the adsorption and desorption process, the production of heterogeneous sites and the sensitivity of biomacromolecule to denaturation (Bereli et al, 2008;Ouyang et al, 2008;Jin and Tang, 2009;Flavin and Resmini, 2009). To resolve these problems, surface polymerization has been proposed to prepare the MIPs film on a solid support substrate, which can improve mass transfer and reduce permanent entrapment of the template, but these methods also reduce the number of imprinting sites (Boninia et al, 2007;Wang et al, 2009a,b;Zhai et al, 2009).…”
Section: Introductionmentioning
confidence: 97%
“…[3][4][5] The imprinting of a particular protein as an artificial antibody is meaningful in the fields of proteomics and biomedicine but still presents challenges due to a number of key inherent problems related to the molecular size, complexity, conformational flexibility, and solubility of the protein. [6][7][8][9][10][11] Owing to the uniquely predetermined selectivity of the MIP protein, diverse strategies have been addressed for protein imprinting, such as bulk polymerization (3D imprinting), [12] surface polymerization (2D imprinting), [13][14][15][16] and the epitope approach. [17,18] One approach of specific interest is the use of a MIP as a HPLC stationary phase for the separation of a target protein.…”
Section: Introductionmentioning
confidence: 99%
“…Those five peptides, such as (N-Acr-l-Cys-NHBn) 2 , are linear or conformational epitopes of the anthrax-protective antigen PA 83 , which made the resulting epitope-cavity show high affinity for the corresponding template, as shown in Tables 9.3 and 9.4. The affinities of the peptide to their corresponding MIPs were more closely related to the molecular weight of the analyte than to the number of residues.…”
Section: Mass-sensitive Devicesmentioning
confidence: 99%
“…The affinities of the peptide to their corresponding MIPs were more closely related to the molecular weight of the analyte than to the number of residues. All epitope-cavities differentiated their epitope region on the protective antigen PA 83 as well as the corresponding furin-cleavage fragments PA 63 and PA 20 . The differential response to the protective antigen fragment could be observed in the picomolar range.…”
Section: Mass-sensitive Devicesmentioning
confidence: 99%
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