Protein adsorbers from surface-grafted copolymers with selective binding sites

He, Dongming; Sun, Weijian; Schräder, Thomas; Ulbricht, Mathias

doi:10.1039/b810752a

Cited by 28 publications

(27 citation statements)

References 28 publications

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“…High affinity and specificity could be achieved with antibody-based systems, with the disadvantage of high price and restriction caused by limited choice of adsorbent. [2] Synthetic protein adsorbents would be cost effective, but suffer from a lack of selectivity and biocompatibility. Proteins tend to be retained onto hydrophobic surfaces and to undergo significant conformational change due to hydrophobic interactions, [3] and adsorptioninduced changes in the structure and dynamics of proteins are observed, which may reduce the biological activity of the proteins.…”

Section: Introductionmentioning

confidence: 99%

Functionalization of MWNTs with Hyperbranched PEI for Highly Selective Isolation of BSA

Chen

et al. 2010

Macromolecular Bioscience

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Cationic hyperbranched BPEI was immobilized on the surface of MWNTs via electrostatic interactions between the positively charged protonated amines within the polymer and the carboxyl groups on the chemically oxidized MWNT surface. The functionalized BPEI-MWNTs were characterized by FT-IR, TGA, TEM and surface charge analysis, and it was used as a bio-sorbent for the adsorption of proteins. CD spectra showed no conformational change of BSA during the adsorption/desorption process. A dynamic adsorption capacity of 167 mg · g⁻¹ for BSA was achieved. With a sample volume of 2.0 mL, an enrichment factor of 10 was obtained along with an adsorption efficiency of 100%, a recovery of 100%, a sampling frequency of 10 h⁻¹ and a RSD of 2.6% at 25 µg · mL⁻¹ BSA.

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Section: Introductionmentioning

confidence: 99%

Functionalization of MWNTs with Hyperbranched PEI for Highly Selective Isolation of BSA

Chen

et al. 2010

Macromolecular Bioscience

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“…However, this leads to the poor mass transport and permanent entrapment by protein imprinting, because the protein is much bigger than the template of typical small molecule 12 imprinting. The slow leakage of the template and poor diffusion of the analyte can result in poor recognition properties.…”

Section: Obstacles Of Protein Imprintingmentioning

confidence: 99%

“…Protein binding in 3D grafted polymer layers has been discussed by Kato et al [134] If the density of polymer chain is less dense, the polymer chains collapse on surface, the adsorption of protein by polymer chains is favored to form 57 surface interaction ("2D model"). [12] This is considered to be an obstacle for effective protein imprinting, because only part of the protein surface has been imprinted. 58 …”

Section: Atrp Initiator Immobilization On Pet Membranementioning

confidence: 99%

Protein-selective adsorbers by molecular imprinting via a novel two-step surface grafting method

Yin

Ulbricht

2013

J. Mater. Chem. B

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Molecularly imprinted polymers (MIP) offer in principle a robust, cost-efficient alternative to antibodies, but it is still a challenge to develop such materials for protein recognition. Here we report the molecular imprinting of a functional polymeric hydrogel layer with whole protein lysozyme as template in two-step grafting procedure by a novel initiation approach on track-etched (TE) polyethylene terephthalate (PET) and cellulose membrane surfaces.This two-step grafting strategy is based on surface functionalization with aliphatic C-Br groups which can be used as initiator for surface-initiated atom transfer radical polymerization (SI-ATRP) and photo-initiated copolymerization. At first, the scaffold poly(methacrylic acid) (PMAA) was obtained through SI-ATRP of poly(tert.-butyl methacrylate) (PtBMA) and subsequent hydrolysis. Thereafter, it was assembled with the template to form a stable PMAA/protein complex. In the second step, a polyacrylamide I declare that this dissertation represents my own work, except where due acknowledgement is made.

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“…[25] Finally, serine and threonine can reversibly form stable esters with aminomethylphenylboronic acid (AMPBA). [46] The Phe-Tyr dipeptide is imitated by aniline and tyramine attached to a triazine core (ApA monomer). [47] Water solubility of the resulting copolymers is secured by the presence of hydroxyl-rich monomers based on hydroxypropylamine (HPA) or glucosamine (Glucosyl), and the dansyl moiety acts as a fluorescent label (dansyl).…”

Section: Comonomer Designmentioning

confidence: 99%

Affinity Polymers Tailored for the Protein A Binding Site of Immunoglobulin G Proteins

Latza¹,

Gilles²,

Schaller³

et al. 2014

Chemistry A European J

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Rational design in combination with a screening process was used to develop affinity polymers for a specific binding site on the surface of immunoglobulin G (IgG) proteins. The concept starts with the identification of critical amino acid residues on the protein interface and their topological arrangement. Appropriate binding monomers were subsequently synthesized. Together with a sugar monomer (2-5 equiv) for water solubility and a dansyl monomer (0.5 equiv) as a fluorescent label, they were subjected in aqueous solution to linear radical copolymerization in various compositions (e.g., azobisisobutyronitrile (AIBN), homogeneous water/DMF mixtures). After ultrafiltration and lyophilization, colorless dry water-soluble powders were obtained. NMR spectroscopic and gel permeation chromatography (GPC) characterization indicated molecular weights between 30 and 500 kD and confirmed retention of monomer composition as well as the absence of monomers. In a competitive enzyme-linked immunosorbent assay (ELISA) screen of the polymer libraries (20-50 members), few copolymers qualified as strong and selective binders for the protein A binding site on the Fc fragment of the antibody. Their monomer composition precisely reflected the critical amino acids found at the interface. The simple combination of a charged and a nonpolar binding monomer sufficed for selective submicromolar IgG recognition by the synthetic polymer. Affinities were confirmed by fluorescence titrations; they increased with decreasing salt load but remained largely unaltered at lowered pH. Other proteins, including those of similar size and isoelectric point (pI), were bound 10-1000 times less tightly. This example indicates that interaction domains in other proteins may also be targeted by synthetic polymers if their comonomer composition reflects the nature and arrangement of amino acid residues on the protein surface.

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Protein adsorbers from surface-grafted copolymers with selective binding sites

Cited by 28 publications

References 28 publications

Functionalization of MWNTs with Hyperbranched PEI for Highly Selective Isolation of BSA

Functionalization of MWNTs with Hyperbranched PEI for Highly Selective Isolation of BSA

Protein-selective adsorbers by molecular imprinting via a novel two-step surface grafting method

Affinity Polymers Tailored for the Protein A Binding Site of Immunoglobulin G Proteins

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