Peptide Imprinted Polymer Nanoparticles: A Plastic Antibody

Hoshino, Yu; Kodama, Takashi; Okahata, Yoshio; Shea, Kenneth J.

doi:10.1021/ja8062875

Cited by 389 publications

(364 citation statements)

References 22 publications

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“…However, the combined affinity and specificity of the NPs were not sufficient to detoxify melittin in animal models. Recently, we demonstrated that by applying a molecular imprinting (19) or an affinity purification process (20) together with the combination of functional monomers, NPs with greater affinity to the target peptide was achieved. Furthermore, the NPs with enhanced binding affinity showed neutralization of the toxin in vivo (3).…”

mentioning

confidence: 99%

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.

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178

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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mentioning

confidence: 99%

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.

Self Cite

178

213

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“…Figure 3e and f indicate that the surface morphology of the pore structures after adsorption of the NPs were less angulated than the surface morphology before adsorption, although none of the pores were filled by the NPs. The apparent surface roughness of the NPs-immobilized pore surface seemed to be comparable to that of the mono-layered dried NPs films (o10 nm), 10,19,20 suggesting that the surface of GBs were coated with NPs. From those results, it was established that NP-adsorbed macroporous GBs could be prepared simply by incubating negatively charged NPs and positively charged GBs in water.…”

Section: Fusion Of Nano and Micro Gel Materials Y Hoshino Et Almentioning

confidence: 86%

“…[5][6][7][8] Shea and colleagues reported that multifunctional nanogel particles (NPs) polymerized with a combination of functional monomers capture target peptides, 9-12 proteins [13][14][15] and specific domains of proteins 16 via a combination of multipoint electrostatic, hydrophobic, aromatic 17 and/or hydrogen binding 18 interactions. Target affinity can be enhanced by optimizing the feed ratio of functional monomers, 19 by molecular imprinting polymerization 20,21 and/or by affinity purification procedures. 22 It has also been reported that porous membranes polymerized with functional monomers containing carbohydrates can be used as affinity separation media for lectins.…”

Section: Introductionmentioning

confidence: 99%

Preparation of nanogel-immobilized porous gel beads for affinity separation of proteins: fusion of nano and micro gel materials

Hoshino

Arata

Yonamine

et al. 2014

Polym J

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We describe the preparation and evaluation of nanogel-immobilized porous gel beads (GB) for application as a protein purification medium. Nanogel particles (NP) that bind with the Fc fragment of immunoglobulin G (IgG) were immobilized on the pore surface of macroporous hard GB containing quaternary ammonium cations on the surface via multipoint electrostatic interactions. The amount of NPs that were irreversibly immobilized in 1 ml of GB slurry was determined to be~30 mg using fluorescent-labeled NPs. Images obtained via scanning electron microscopy established that the NPs were uniformly immobilized on the surface of the pores without blocking the macropores. The model target protein (IgG) was reversibly captured by the NPimmobilized GBs through NP-IgG interactions. NP-immobilized GBs have potential applications as novel affinity purification media for proteins, combining inexpensive and stable ligands with high-performance supports.

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“…The polymer composition for the preparation of the nanoMIPs was adapted from Hoshino and colleagues. 22 In addition to this, nanoparticles for melamine were prepared in an organic solvent (ACN) by UV polymerisation with and without a PEG shell. In general the interactions between all the imprinted polymers nanoparticles and the different templates were due to a combination of multiple electrostatic and hydrophobic interactions.…”

Section: Synthesis and Characterisation Of Nanomipsmentioning

confidence: 99%

“…18 Recently, several research groups have reported examples of protocols for the synthesis of MIP nanoparticles. [19][20]22 In our case the nanoparticles, which can be produced either in aqueous or organic media depending on the template molecule, exhibit uniform binding sites and high affinity for the target analyte. The main advantage of materials prepared by such solid-phase approach is the possibility to replace directly antibodies with MIPs in standard pseudo-ELISA, with minimal modification of the immobilisation and assay protocol.…”

Section: Introductionmentioning

confidence: 99%

Does size matter? Study of performance of pseudo-ELISAs based on molecularly imprinted polymer nanoparticles prepared for analytes of different sizes

Cáceres

Canfarotta

Chianella

et al. 2016

Analyst

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Abstract. The aim of this work is to evaluate whether the size of the analyte used as template for the synthesis of molecularly imprinted polymer nanoparticles (nanoMIPs) can affect their performance in pseudo-enzyme linked immunosorbent assays (pseudo-ELISAs). Successful demonstration of a nanoMIPs-based pseudo-ELISA for vancomycin (1449.3 g mol -1 ) was demonstrated earlier. In the present investigation, the following analytes were selected: horseradish peroxidase (HRP, 44 kDa), cytochrome C (Cyt C, 12 kDa) biotin (244.31 g mol -1 ) and melamine (126.12 g mol -1 ). NanoMIPs with a similar composition for all analytes were synthesised by persulfate-initiated polymerisation in water. In addition, core-shell nanoMIPs coated with polyethylene glycol (PEG) and imprinted for melamine were produced in organics and tested. The polymerisation of the nanoparticles was done using a solid-phase approach with the correspondent template immobilised on glass beads. The performance of the nanoMIPs used as replacement for antibodies in direct pseudo-ELISA (for the enzymes) and competitive pseudo-ELISA for the smaller analytes was investigated. For the competitive mode we rely on competition for the binding to the nanoparticles between free analyte and corresponding analyte-HRP conjugate. The results revealed that the best performances were obtained for nanoMIPs synthesised in aqueous media for the larger analytes. In addition, this approach was successful for biotin but completely failed for the smallest template melamine. This problem was solved using nanoMIP prepared by UV polymerisation in an organic media with a PEG shell. This study demonstrates that the preparation of nanoMIP by solid-phase approach can produce material with high affinity and potential to replace antibodies in ELISA tests for both large and small analytes. This makes this technology versatile and applicable to practically any target analyte and diagnostic field.

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Peptide Imprinted Polymer Nanoparticles: A Plastic Antibody

Cited by 389 publications

References 22 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

Preparation of nanogel-immobilized porous gel beads for affinity separation of proteins: fusion of nano and micro gel materials

Does size matter? Study of performance of pseudo-ELISAs based on molecularly imprinted polymer nanoparticles prepared for analytes of different sizes

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