4.5 Article

Out of Pocket Protein Binding-A Dilemma of Epitope Imprinted Polymers Revealed for Human Hemoglobin

期刊

CHEMOSENSORS
卷 9, 期 6, 页码 -

出版社

MDPI
DOI: 10.3390/chemosensors9060128

关键词

Molecularly Imprinted Polymers; epitope imprinting; non-specific binding; redox gating; SEIRA spectroelectrochemistry

资金

  1. Deutsche Forschungsgemeinschaft (D.F.G., German Research Foundation) [EXC 2008-390540038-UniSysCat]
  2. EU within the European Union's Horizon 2020 research and innovation program [810856]
  3. Einstein Foundation Berlin [EVF-2016-277]
  4. BME Nanotechnology and Materials Science TKP2020 IE grant of NKFIH Hungary (BME IE-NATTKP2020)

向作者/读者索取更多资源

The study utilized epitope imprinting polymers to recognize parent proteins, revealing non-specific binding between target peptides and parent proteins, as well as stronger non-specific binding of HbA to MIPs than target peptides.
The epitope imprinting approach applies exposed peptides as templates to synthesize Molecularly Imprinted Polymers (MIPs) for the recognition of the parent protein. While generally the template protein binding to such MIPs is considered to occur via the epitope-shaped cavities, unspecific interactions of the analyte with non-imprinted polymer as well as the detection method used may add to the complexity and interpretation of the target rebinding. To get new insights on the effects governing the rebinding of analytes, we electrosynthesized two epitope-imprinted polymers using the N-terminal pentapeptide VHLTP-amide of human hemoglobin (HbA) as the template. MIPs were prepared either by single-step electrosynthesis of scopoletin/pentapeptide mixtures or electropolymerization was performed after chemisorption of the cysteine extended VHLTP peptide. Rebinding of the target peptide and the parent HbA protein to the MIP nanofilms was quantified by square wave voltammetry using a redox probe gating, surface enhanced infrared absorption spectroscopy, and atomic force microscopy. While binding of the pentapeptide shows large influence of the amino acid sequence, all three methods revealed strong non-specific binding of HbA to both polyscopoletin-based MIPs with even higher affinities than the target peptides.

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