Strategien zur Modulation von Protein‐Protein‐Wechselwirkungen mit synthetischen Substanzen

Yin, Hang; Hamilton, Andrew D.

doi:10.1002/ange.200461786

Cited by 85 publications

(33 citation statements)

References 366 publications

(226 reference statements)

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“…There are two separate, but not unrelated, requirements to create functional materials that incorporate both selective protein affinity and a trigger for the capture and release of the protein cargo. Strong affinity between designed synthetic materials and proteins has been achieved by incorporating complimentary functional groups into synthetic molecular scaffolds, [11] liner polymers, [12] dendritic polymers, [13] and synthetic NPs. [2,3,10] Based upon our experience with protein and peptide binding to synthetic polymers, we employed an approach that imparts a protein binding capability to temperature-responsive NIPAm-based NPs by incorporating functional groups that are complimentary to a target protein.…”

mentioning

confidence: 99%

Temperature‐Responsive “Catch and Release” of Proteins by using Multifunctional Polymer‐Based Nanoparticles

Yoshimatsu¹,

Lesel²,

Yonamine³

et al. 2012

Angew Chem Int Ed

147

101

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mentioning

confidence: 99%

Temperature‐Responsive “Catch and Release” of Proteins by using Multifunctional Polymer‐Based Nanoparticles

Yoshimatsu¹,

Lesel²,

Yonamine³

et al. 2012

Angew Chem Int Ed

147

101

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“…[16][17][18][19] Deliberate and specific interference with synthetic agents, however, has been coined as "high-hanging fruit in drug discovery", [20] and few examples exist that do not rely on library screens. [21][22][23] Several molecular imprinting technologies have been tried on proteins but still suffer from low non-imprinted polymer/molecularly imprinted polymer (NIP/MIP) ratios and incomplete protein recovery; the most promising techniques involve epitope imprinting (most often restricted to N/C termini), hierarchical imprinting, and imprinted soft nanoparticles. [24][25][26] Although artificial epitope-specific materials would have a large number of potential applications, there is a frustrating lack of methods for their generation and manipulation.…”

Section: Introductionmentioning

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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“…One such effort concerned the construction of biologically active molecules by producing specific binding domains or converging appended binding sites in a required space. [7,11] Another important effort has been devoted to their applications in supramolecular chemistry. Along this line, our works and those by other groups on aromatic amide foldamers have demonstrated that this family of folded backbones are robust acyclic receptors for discrete molecular and ionic guests.…”

Section: Introductionmentioning

confidence: 99%

Hydrogen‐Bonding‐Driven Aromatic Foldamers: Their Structural and Functional Evolution

Zhang

Wang

2014

The Chemical Record

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This Personal Account summarizes the development of the design of hydrogen-bonding-driven aromatic foldamers and their applications in supramolecular chemistry. This account begins with a short, non-exhaustive description of the background in the study of hydrogen-bonded aromatic foldamers. The construction of foldamers from discrete aromatic residues, including amide, urea, hydrazide and 1,2,3-triazole units, is then described. In the following parts, the applications of such compact aromatic oligomers in supramolecular chemistry, including the development of acyclic receptors, the construction of hybrid helical sequences through intramolecular stacking, the promotion of the formation of covalently and noncovalently bonded macrocycles, the tuning of the mechanical properties of copolymers, and the regulation of the shuttling behavior of [2]rotaxanes and the controlled release of dye from reverse vesicles formed from them, are described. In the final part, the binding-induced folding of conformationally flexible aromatic amide oligomers and their self-binding are described.

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Strategien zur Modulation von Protein‐Protein‐Wechselwirkungen mit synthetischen Substanzen

Cited by 85 publications

References 366 publications

Temperature‐Responsive “Catch and Release” of Proteins by using Multifunctional Polymer‐Based Nanoparticles

Temperature‐Responsive “Catch and Release” of Proteins by using Multifunctional Polymer‐Based Nanoparticles

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

Hydrogen‐Bonding‐Driven Aromatic Foldamers: Their Structural and Functional Evolution

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