Sequence Selective Binding of Peptides by Artificial Receptors in Aqueous Solution

Breslow, Ronald; Yang, Zhiwei; Ching, Rachel Hiu Ha; Trojandt, Gunter; Odobel, Fabrice

doi:10.1021/ja973991y

Cited by 162 publications

(56 citation statements)

References 11 publications

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“…In any case, it is important to understand how the sequence environment (i.e., neighboring residues) influences binding. Several synthetic receptors have been shown to bind peptides and proteins (4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17), but in the majority of cases, these receptors are known to bind to a single type of residue, and the effects of sequence context are understood to a limited extent. This paper describes the effects of sequence context on the interactions of tryptophan-containing peptides with the synthetic receptor, cucurbit [8]uril (Q8), and a method that enables this determination in a rapid and parallel fashion.…”

Section: Introductionmentioning

confidence: 99%

Effects of sequence context on the binding of tryptophan-containing peptides by the cucurbit[8]uril–methyl viologen complex

Ali

Olson

Urbach

2013

Supramolecular Chemistry

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Section: Introductionmentioning

confidence: 99%

Effects of sequence context on the binding of tryptophan-containing peptides by the cucurbit[8]uril–methyl viologen complex

Ali

Olson

Urbach

2013

Supramolecular Chemistry

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“…b-CD dimers had previously been shown to bind the hydrophobic side chains in polypeptides selectively (Breslow et al 1998), and Breslow et al hoped that these results may be extended to bind hydrophobic residues on the interfacial regions of multimeric proteins, and thereby Targeting protein-protein interactions S. Fletcher and A. D. Hamilton 225 inhibit protein aggregation, hence protein function. A series of 11 cyclodextrin dimers with a variety of linkers and cyclodextrin cavity orientation were prepared, and the abilities of these analogues to disrupt protein aggregation were assessed by monitoring enzyme activity.…”

Section: Cyclodextrinsmentioning

confidence: 99%

Targeting protein–protein interactions by rational design: mimicry of protein surfaces

Fletcher

Hamilton

2006

J. R. Soc. Interface.

155

133

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Protein-protein interactions play key roles in a range of biological processes, and are therefore important targets for the design of novel therapeutics. Unlike in the design of enzyme active site inhibitors, the disruption of protein-protein interactions is far more challenging, due to such factors as the large interfacial areas involved and the relatively flat and featureless topologies of these surfaces. Nevertheless, in spite of such challenges, there has been considerable progress in recent years. In this review, we discuss this progress in the context of mimicry of protein surfaces: targeting protein-protein interactions by rational design.

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“…Interactions of CDs with proteins and peptides have been widely studied. It has been postulated that their interaction with CDs could be local, that is, accessible hydrophobic side chains may form inclusion complexes with CDs, since molecules of many peptides and proteins are too hydrophilic and bulky to be wholly included in the CD cavity and the topological constraints of the peptide backbone may reduce the formation of inclusion complexes [26,27]. Such interactions have been utilized in protein folding, solubilizing and/or stabilizing [28], as well as in delivering proteins and peptides [29].…”

Section: Use Of Cyclodextrinsmentioning

confidence: 99%

Detection of prion protein using a capillary electrophoresis-based competitive immunoassay with laser-induced fluorescence detection and cyclodextrin-aided separation

Yang¹,

Yeung

Schmerr

2005

Electrophoresis

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The development of capillary electrophoresis (CE)-based competitive immunoassay for prion protein (PrP) using carboxymethyl beta-cyclodextrin (CM-beta-CD) as a buffer additive is described here. The assay was based on the competitive binding of PrP and a fluorescein-labeled peptide from the prion protein with a limiting amount of specific antibody. The amount of both free and fluorescein-labeled peptide bound to antibody (immunocomplex) were determined by CE with laser-induced fluorescence detection. In the presence of PrP, the peak height ratio of the immunocomplex and the free peptide was altered compared to the control. These changes were directly proportional to the amount of PrP present. The fluorescently labeled peptide spanning amino acid positions 140-158 of the PrP and its corresponding monoclonal antibody is reported here. The reaction times of the antibody with either the peptide or the recombinant PrP was less than 1 min and is a large improvement over the 16-18 h required to achieve equilibrium for polyclonal antibodies. CM-beta-CD was explored as a buffer additive to suppress analyte adsorption and enhance separation selectivity in the CE analysis. A fast (1.1 min), selective (resolution 4.7), and reproducible (relative standard deviations of migration time for free and bound fluorescein isothiocyanate (FITC)-peptide 0.56% and 0.64%, respectively) separation was obtained with 0.6% CM-beta-CD in 25 mM N-tris(hydroxymethyl)methyl-3-aminopropanesulfonic acid (TAPS) at pH 8.8. The concentration detection limit of the assay for recombinant PrP was determined to be 80 ng/mL (or mass detection limit 1 pg). When blood samples from scrapie-infected sheep and from normal sheep were tested, the results of the blood assay were consistent with scrapie status of the sheep as determined post mortem by Western blot analysis. Development of this assay will lead to a potentially robust, rapid, and specific preclinical diagnosis for transmissible spongiform encephalopathies (TSEs) in animals and humans.

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Sequence Selective Binding of Peptides by Artificial Receptors in Aqueous Solution

Cited by 162 publications

References 11 publications

Effects of sequence context on the binding of tryptophan-containing peptides by the cucurbit[8]uril–methyl viologen complex

Effects of sequence context on the binding of tryptophan-containing peptides by the cucurbit[8]uril–methyl viologen complex

Targeting protein–protein interactions by rational design: mimicry of protein surfaces

Detection of prion protein using a capillary electrophoresis-based competitive immunoassay with laser-induced fluorescence detection and cyclodextrin-aided separation

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