Protein Recognition via Surface Molecularly Imprinted Polymer Nanowires

Li, Yong; Yang, Huang‐Hao; You, Qi Hua; Zhuang, Zhixia; Wang, Xiaoru

doi:10.1021/ac050802i

Cited by 249 publications

(137 citation statements)

References 15 publications

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“…NPs with the highest AAc (40 mol%) and TBAm (40 mol%) (NPs 9) showed the highest melittin-binding capacity, 180 μmol g −1 (0.5 g melittin per a gram of NP). This capacity is 10 5 or 10 2 times larger than that of previously reported protein adsorbing films (5,26) or nano-fibers (27) and more than 10 times greater than that of immunoglobulins (IgGs; 2 binding sites per 150 kDa ¼ 13 μmol g −1 ). The binding capacity indicates that on average a 50 mer polymer fragment captures a molecule of melittin (26 amino acid) ( Table 2), suggesting that most of the polymer chains in NP 9 are in contact with melittin.…”

Section: Resultsmentioning

confidence: 68%

The rational design of a synthetic polymer nanoparticle that neutralizes a toxic peptide in vivo

Hoshino

Koide

Furuya

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

174

213

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Synthetic polymer nanoparticles (NPs) that bind venomous molecules and neutralize their function in vivo are of significant interest as "plastic antidotes." Recently, procedures to synthesize polymer NPs with affinity for target peptides have been reported. However, the performance of synthetic materials in vivo is a far greater challenge. Particle size, surface charge, and hydrophobicity affect not only the binding affinity and capacity to the target toxin but also the toxicity of NPs and the creation of a "corona" of proteins around NPs that can alter and or suppress the intended performance. Here, we report the design rationale of a plastic antidote for in vivo applications. Optimizing the choice and ratio of functional monomers incorporated in the NP maximized the binding affinity and capacity toward a target peptide. Biocompatibility tests of the NPs in vitro and in vivo revealed the importance of tuning surface charge and hydrophobicity to minimize NP toxicity and prevent aggregation induced by nonspecific interactions with plasma proteins. The toxin neutralization capacity of NPs in vivo showed a strong correlation with binding affinity and capacity in vitro. Furthermore, in vivo imaging experiments established the NPs accelerate clearance of the toxic peptide and eventually accumulate in macrophages in the liver. These results provide a platform to design plastic antidotes and reveal the potential and possible limitations of using synthetic polymer nanoparticles as plastic antidotes.

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Section: Resultsmentioning

confidence: 68%

The rational design of a synthetic polymer nanoparticle that neutralizes a toxic peptide in vivo

Hoshino

Koide

Furuya

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

174

213

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“…The protein binding and removal process at MIP and NIP electrodes were characterized by cyclic voltammetry in 10 mM K 4 Fe(CN) 6 in PBS at pH 7.4 in the range of -0.2 to 0.6 V at a scan rate of 50 mV/s. For protein binding the MIPs and NIPs were equilibrated in the ferrocyanide solution where a reference CV was recorded, followed by addition of HSA or ferritin.…”

Section: Electrochemical Detection Of the Mip-target Bindingmentioning

confidence: 99%

“…Electrochemical template removal [41] was performed by immersing the polymer-modified electrode in 0.1 M H 2 SO 4 and cycling the potential between -0.2 and 1.5 V at 200 mV/s and the CV of 10 mM K 4 Fe(CN) 6 was obtained intermittently to monitor the progression of the template removal. A sudden increase in the peak current was observed between 30 and 40 removal cycles indicating the necessity to perform at least 40 cycles to quantitatively remove the template (Figure 3a).…”

Section: Template Removalmentioning

confidence: 99%

“…Subsequent removal of the template leads to recognition sites in the molecularly imprinted polymer (MIP) that can selectively rebind the target. Extending this principle to macromolecules such as proteins necessitated the implementation of a variety of enabling technologies (e.g., epitope imprinting, [4,5] surface imprinting [6][7][8][9][10]) to cope both with the fragility of the target [11] as well as with its limited diffusivity in the cross-linked polymeric matrices. The electrochemical polymerization in this respect offers clear advantages such as performing the polymerization in aqueous conditions that is compatible with the proteinaceous target.…”

Section: Introductionmentioning

confidence: 99%

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Electrosynthesized molecularly imprinted polyscopoletin nanofilms for human serum albumin detection

Stojanović

Erdőssy

Keltai

et al. 2017

Analytica Chimica Acta

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Molecularly imprinted polymers (MIPs) rendered selective solely by the imprinting with protein templates lacking of distinctive properties to facilitate strong target-MIP interaction are likely to exhibit medium to low template binding affinities. While this prohibits the use of such MIPs for applications requiring the assessment of very low template concentrations, their implementation for the quantification of high-abundance proteins seems to have a clear niche in the analytical practice. We investigated this opportunity by developing a polyscopoletin-based MIP nanofilm for the electrochemical determination of elevated human serum albumin (HSA) in urine. As reference for low abundance protein ferritin-MIPs were 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 23 24 25 26 27 28 29 30 31 32 33 34 35 36 37 38 39 40 41 42 43 44 45 46 47 48 49 50 51 52 53 54 55 56 57 58 59 60 61 62 63 64 65 2 also prepared by the same procedure. Under optimal conditions, the imprinted sensors gave a linear response to HSA in the concentration range of 20-100 mg/dm 3 , and to ferritin in the range of 120-360 mg/dm 3 . While as expected the obtained limit of detection was not sufficient to determine endogenous ferritin in plasma, the HSA-sensor was successfully employed to analyse urine samples of patients with albuminuria. The results suggest that MIP-based sensors may be applicable for quantifying high abundance proteins in a clinical setting.

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“…These include mostly chemical treatments that look for protein denaturation and amide bond cleavage [57][58][59][60][61]. Most recently, we have proposed the use of enzymes displaying proteolytic activity capable of cleaving peptide bonds [28].…”

Section: Protein Removalmentioning

confidence: 99%

Protein-responsive polymers for point-of-care detection of cardiac biomarker

Moreira

Sharma

Dutra

et al. 2014

Sensors and Actuators B: Chemical

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This work describes a novel use for the polymeric film, poly(o-aminophenol) (PAP) that was made respon-sive to a specific protein. This was achieved through templated electropolymerization of aminophenol (AP) in the presence of protein. The procedure involved adsorbing prot ein on the electrode surface and thereafter electroploymerizing the aminophenol. Proteins embedded at the outer surface of the polymeric film were digested by proteinase K and then washed away thereby creating vacant sites. The capacity of the template film to specifically rebind protein was tested with myoglobin (Myo), a cardiac biomarker for ischemia. The films acted as biomimetic artificial antibodies and were produced on a gold (Au) screen printed electrode (SPE), as a step towards disposable sensors to enable point-of-care applications.Raman spectroscopy was used to follow the surface modification of the Au-SPE. The ability of the mate-rial to rebind Myo was measured by electrochemical techniques, namely electrochemical impedance spectroscopy (EIS) and square wave voltammetry (SWV). The d evices displayed linear responses to Myo in EIS and SWV assays down to 4.0 and 3.5 µg/mL, respectively, with detection limits of 1.5 and 0.8 µg/mL. Good selectivity was observed in the presence of troponin T (TnT) and creatine kinase (CKMB) in SWV assays, and accurate results were obtained in applications to spiked serum. The sensor described in this work is a potential tool for screening Myo in point-of-care due to the simplicity of fabrication, disposability, short time response, low cost, good sensitivit y and selectivity.

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Protein Recognition via Surface Molecularly Imprinted Polymer Nanowires

Cited by 249 publications

References 15 publications

The rational design of a synthetic polymer nanoparticle that neutralizes a toxic peptide in vivo

The rational design of a synthetic polymer nanoparticle that neutralizes a toxic peptide in vivo

Electrosynthesized molecularly imprinted polyscopoletin nanofilms for human serum albumin detection

Protein-responsive polymers for point-of-care detection of cardiac biomarker

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