Selective Protein Capture by Epitope Imprinting

Nishino, Hidekazu; Huang, Chin-Shiou; Shea, Kenneth J.

doi:10.1002/ange.200503760

Cited by 105 publications

(87 citation statements)

References 24 publications

(1 reference statement)

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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 optimized NPs showed a much higher apparent binding constant (6.6 × 10 7 M −1 ) than NPs reported earlier (1.6 × 10 6 M −1 ) (6) and had an extremely high binding capacity (180 μmol g −1 ) that is greater than 10 fold larger than IgG (13 μmol g −1 ). Our results revealed the greater capacity is due to the higher surface to volume ratio of the nano-size materials than the bulk polymer films (5,26). Melittin might also diffuse into and be captured in the interior of the NP since the particles are hydrogels consisting of >70% water (19).…”

Section: Discussionmentioning

confidence: 82%

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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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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%

Section: Discussionmentioning

confidence: 82%

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

174

213

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show abstract

“…Artificial antibody copies are an alternative for direct imprinting if the analyte is unstable and will denature during the imprinting process. Additionally, instead of the whole analyte that is recognized in conventional imprinting, artificial antibodies have an epitope which generally leads to less cross reactivity in substructure imprinting [29].…”

Section: Discussionmentioning

confidence: 99%

“…In contrast to conventional imprinting where the whole template is recognized, double imprinted surfaces (as natural antibodies) recognize epitopes (substructures of a molecule) [28]. This is believed to be favourable for recognition of large and complex biomolecules [29]. This method has so far only been used for aqueous solutions.…”

Section: Introductionmentioning

confidence: 99%

Immunosensing with artificial antibodies in organic solvents or complex matrices

Schirhagl

Qian

Dickert

2012

Sensors and Actuators B: Chemical

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a b s t r a c tThe detection of analytes in complex matrices without labour intensive sample preparation is an important goal in analytical chemistry. In this article we would like to address this issue by transferring the selectivity of natural antibody in a cheap, robust and reusable polymer, employing a double imprinting protocol. Antibodies with the desired selectivity were used as template to generate imprinted polymer particles. These antibodies were added to a prepolymer and particles were precipitated. After the antibodies were removed from the particles, cavities remained which reproduce size, shape and surface chemistry of the antibodies. In a second imprinting step the particles with cavities were pressed into a second polymer. After the second polymer has cured the particles can be removed leaving positive structures behind that react with the desired antigen. Such a sensitive coating was applied to the surface of a quartz crystal microbalance and incorporated into a microfluidic chip. An immunosensor for estradiol was fabricated having six times higher affinity to its antigen than to structurally related molecules. The measurements can also be performed after an extraction into an organic solvent which improves the detection limit greatly and would not be possible for natural antibodies. The feasibility of the method for complex matrices was shown by detecting viruses in plasma or allergenic protein in bread extract.

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“…Compared size and the incompatibility between the fragile protein template and the imprinting conditions. To resolve these issues, various approaches have been proposed for the successful imprinting of proteins, such as surface imprinting [8,9], epitope-mediated imprinting [10,11], covalent imprinting [12], and the use of low cross-linking density hydrogels [13,14].…”

Section: Introductionmentioning

confidence: 99%

Smart surface imprinting polymer nanospheres for selective recognition and separation of glycoprotein

Gao

et al. 2013

Colloids and Surfaces A: Physicochemical and Engineering Aspect

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Selective Protein Capture by Epitope Imprinting

Cited by 105 publications

References 24 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

Immunosensing with artificial antibodies in organic solvents or complex matrices

Smart surface imprinting polymer nanospheres for selective recognition and separation of glycoprotein

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