In situ formation of polymer–protein hybrid spherical aggregates from (nitrilotriacetic acid)-end-functionalized polystyrenes and His-tagged proteins

Kadir, Mohammad Abdul; Lee, Chaeyeon; Han, Ho Seok; Kim, Bongsoo; Ha, Eun-Ju; Jeong, Jong Hwa; Song, Jae Kwang; Lee, Sun‐Gu; An, Seong Soo A.; Paik, Hyun‐jong

doi:10.1039/c2py21077k

Cited by 16 publications

(16 citation statements)

References 57 publications

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“…Protein–polymer hybrids (PPHs) can result in the formation of a rich variety of microdomain morphologies such as spheres, vesicles, and long bundles of fibers . As conjugation of temperature‐responsive polymer to protein, mCherry‐pNIPAAm hybrid was self‐assembled into the highly disordered lamellae or hexagonally perforated lamellae depending upon the selectivity of the solvent during evaporation, and Vault‐pNIPAAm hybrid was self‐assembled into the nanocapsules, which underwent reversible aggregation upon heating above LCST of pNIPAAm …”

Section: Resultsmentioning

confidence: 99%

Temperature‐responsive “tadpole‐shaped” protein–polymer hybrids and their self‐assembly behavior

Wang

2016

Polymers for Advanced Techs

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The temperature‐responsive poly (N, N‐diethylacrylamide) (pDEAAm) with narrower molecular weight distribution was prepared by the atom transfer radical polymerization and characterized by 1HNMR and gel permeation chromatography. The temperature‐responsive “tadpole‐shaped” BSA–pDEAAm hybrids were fabricated via a free Cys‐34 residue of bovine serum albumin (BSA) site specifically binding to the end group disulfide bonds of pDEAAm and characterized by native‐polyacrylamide gel electrophoresis (Native‐PAGE) and matrix‐assisted laser desorption/ionization time of flight mass spectrometry. Their temperature‐responsive behaviors were measured by ultraviolet‐visible spectra (UV‐Vis). The lower critical solution temperature (LCST) of the pDEAAm was identified as 28°C, and the LCST of BSA–pDEAAm hybrids was identified as 31°C. The morphologies of BSA–pDEAAm hybrids self‐assembled in the aqueous solutions with two different temperatures at 25 °C and 40°C were investigated by transmission electron microscopy. Below the LCST of BSA–pDEAAm hybrids, the separate spherical nanoparticles were observed. In contrast, bundles and clusters were observed above the LCST of BSA–pDEAAm hybrids. The results suggested that the self‐assembly morphology of BSA–pDEAAm hybrids depended upon the pDEAAm block in BSA–pDEAAm hybrids, and the morphology transitions were effected by the LCST of BSA–pDEAAm hybrids. It would be expected to be used in biomedicine and materials science. Copyright © 2016 John Wiley & Sons, Ltd.

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Section: Resultsmentioning

confidence: 99%

Temperature‐responsive “tadpole‐shaped” protein–polymer hybrids and their self‐assembly behavior

Wang

2016

Polymers for Advanced Techs

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“…The complexation of polystyrene and protein is used for the synthesis of the protein nanoparticles [ 30 , 31 , 32 ]. Figure 1 shows the conjugation of polymer containing nitrilotriacetic acid end-functionalized polystyrene (NTA-PS) and histidine-tagged green fluorescence protein (His-GFP).…”

Section: Synthesis Of Materialsmentioning

confidence: 99%

“…The Ni 2+ complexation with the histidine is fast and reversible. Imidazole can displace the His-tag proteins [ 30 , 32 ].…”

Section: Synthesis Of Materialsmentioning

confidence: 99%

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Preparation of Protein Nanoparticles Using NTA End Functionalized Polystyrenes on the Interface of a Multi-Laminated Flow Formed in a Microchannel

et al. 2017

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This paper challenges the production of the protein nanoparticles using the conjugation of Ni2+ complexed nitrilotriacetic acid end-functionalized polystyrene (Ni-NTA-PS) and histidine tagged GFP (His-GFP) hybrid. The microfluidic synthesis of the protein nanoparticle with the advantages of a uniform size, a fast reaction, and a precise control of preparation conditions is examined. The self-assembly occurs on the interfacial surface of the multi-laminated laminar flow stably formed in the microchannel. The clogging of the produced protein nanoparticles on the channel surface is solved by adding a retarding inlet channel. The size and shape of the produced protein nanoparticles are measured by the analysis of transmission electron microscopy (TEM) and scanning electron microscope (SEM) images, and the attachment of the protein is visualized with a green fluorescent image. Future research includes the encapsulation of vaccines and the coating of antigens on the protein surface.

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“…Recently, our group also reported the synthesis of nickel‐complexed mono‐NTA‐end‐functionalized polystyrenes by ATRP and demonstrated their diverse applications in bioconjugation with His‐tagged proteins, encapsulation of NPs, selective purification of His‐tagged proteins, construction of polymer–protein hybrid nanostructures, and controlled dispersion of single‐walled carbon nanotubes . Herein, we reported the synthesis of NTA‐end‐functionalized polystyrenes (tri‐NTA‐PS) by atom transfer radial polymerization (ATRP) of styrene, which produced self‐assembled spherical aggregates with ≈40–60 nm diameters in water/THF, while His‐tagged GFP produced spherical core–shell hybrid aggregates with ≈90–115 nm diameters in water/DMF (DMF 4 vol%) through NTA‐Ni/His interactions.…”

Section: Introductionmentioning

confidence: 99%

Multivalent (Nitrilotriacetic Acid)‐End‐Functionalized Polystyrenes by ATRP and Their Self‐Assembly

Kadir

Park

Lee

et al. 2013

Macro Chemistry & Physics

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The synthesis of tri‐(nitrilotriacetic acid) (NTA)‐end‐functionalized polystyrenes using an initiator containing tert‐butyl protected NTA moieties, by atom transfer radical polymerization (ATRP) of styrene is described. First, a suitable ATRP initiator is prepared and subsequently characterized by 1H and 13C NMR spectroscopy, gel‐permeation chromatography (GPC), and matrix‐assisted laser desorption ionization time‐of‐flight (MALDI‐TOF) mass spectroscopy. The structures of the tri‐NTA‐end‐functionalized polystyrenes (tri‐NTA‐PS) are confirmed by 1H and 13C NMR spectroscopy. Tri‐NTA‐PS itself produces self‐assembled spherical aggregates with ≈40–60 nm diameters in water/THF, whereas nickel‐complexed tri‐NTA‐PS produces spherical core–shell hybrid aggregates with ≈90–115 nm diameters with His‐tagged GFP in water/DMF (DMF 4 vol%), as confirmed by transmission electron microscopy and dynamic light scattering measurements.

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In situ formation of polymer–protein hybrid spherical aggregates from (nitrilotriacetic acid)-end-functionalized polystyrenes and His-tagged proteins

Cited by 16 publications

References 57 publications

Temperature‐responsive “tadpole‐shaped” protein–polymer hybrids and their self‐assembly behavior

Temperature‐responsive “tadpole‐shaped” protein–polymer hybrids and their self‐assembly behavior

Preparation of Protein Nanoparticles Using NTA End Functionalized Polystyrenes on the Interface of a Multi-Laminated Flow Formed in a Microchannel

Multivalent (Nitrilotriacetic Acid)‐End‐Functionalized Polystyrenes by ATRP and Their Self‐Assembly

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