Arginine mimetic appended peptide-based probes for fluorescence turn-on detection of 14-3-3 proteins

Maity, Debabrata; Gigante, Alba; Sánchez‐Murcia, Pedro A.; Sijbesma, Eline; Li, Mao; Bier, David; Mosel, Stefanie; Knauer, Shirley K.; Ottmann, C.; Schmuck, Carsten

doi:10.1039/c9ob00620f

Cited by 13 publications

(12 citation statements)

References 25 publications

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“…Binding to 14‐3‐3 proteins is mediated by short peptide sequences featuring phosphorylated serines or threonines (pS or pT) in the partner proteins . A few compounds are already reported for the modulation of interactions of 14‐3‐3 proteins, like natural products, such as fusicoccin and cotylenin A, as well as synthetic compounds as molecular tweezers and supramolecular ligands . However, there is still a lack of bottom‐up design principles for designing specific stabilizers of the 14‐3‐3 family.…”

Section: Figurementioning

confidence: 99%

Multivalent Ligands with Tailor‐Made Anion Binding Motif as Stabilizers of Protein–Protein Interactions

et al. 2019

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Modulation of protein–protein interactions (PPIs) is essential for understanding and tuning biologically relevant processes. Although inhibitors for PPIs are widely used, the field still lacks the targeted design of stabilizers. Here, we report unnatural stabilizers based on the combination of multivalency effects and the artificial building block guanidiniocarbonylpyrrol (GCP), an arginine mimetic. Unlike other GCP‐based ligands that modulate PPIs in different protein targets, only a tetrameric design shows potent activity as stabilizer of the 14‐3‐3ζ/C‐Raf and 14‐3‐3ζ/Tau complexes in the low‐micromolar range. This evidences the role of multivalency for achieving higher specificity in the modulation of PPIs.

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Section: Figurementioning

confidence: 99%

Multivalent Ligands with Tailor‐Made Anion Binding Motif as Stabilizers of Protein–Protein Interactions

et al. 2019

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“…Overall, the AIE effect observed for our oligomers is not extremely high yet significant and well in the range of other ligands described in literature that have successfully used emission changes to detect ligand binding. [35,36] Figure 3 highlights the differences between O4 (Figure 3B), and O5 (Figure 3C) as exemplary non-AIE oligomer when binding to MGs and PAA. Also optically, the AIE effects were clearly visible for O4 in contrast to O5 with no increase in emission upon mixing with any of the anionic compounds.…”

Section: Resultsmentioning

confidence: 99%

Take your Positions and Shine: Effects of Positioning Aggregation‐Induced Emission Luminophores within Sequence‐Defined Macromolecules

Pasch

Killa

Junghans

et al. 2021

Chemistry A European J

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A luminophore with aggregation‐induced emission (AIE) is employed for the conjugation onto supramolecular ligands to allow for detection of ligand binding. Supramolecular ligands are based on the combination of sequence‐defined oligo(amidoamine) scaffolds and guanidiniocarbonyl‐pyrrole (GCP) as binding motif. We hypothesize that AIE properties are strongly affected by positioning of the luminophore within the ligand scaffold. Therefore, we systematically investigate the effects placing the AIE luminophore at different positions within the overall construct, for example, in the main or side chain of the olig(amidoamine). Indeed, we can show that the position within the ligand structure strongly affects AIE, both for the ligand itself as well as when applying the ligand for the detection of different biological and synthetic polyanions.

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“…[46]. Therefore, the Schmuck group in collaboration with the Ottmann group sought to develop fluorescent probes (7 and 8) for monitoring of 14-3-3 proteins ( Figure 7) [47]. These probes contain two symmetric GCP-Phe/Trp-Lys-Gly peptidic arms and an artificial anion binding GCP moiety at both termini for 14-3-3 proteins recognition.…”

Section: -3-3 Proteinsmentioning

confidence: 99%

“…A) Molecular structure of peptidic probes 7 and 8; B) fluorescence emission spectra of probe 7 (5.0 µM) with increasing concentration (0-5.0 µM) of 14-3-3β protein (λ ex = 410 nm). Inset: Corresponding fluorescence color of the solution inside cuvette under UV lamp.Reproduced from[47] with permission from The Royal Society of Chemistry.…”

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Selected peptide-based fluorescent probes for biological applications

Maity¹

2020

Beilstein J. Org. Chem.

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To understand the molecular interactions, present in living organisms and their environments, chemists are trying to create novel chemical tools. In this regard, peptide-based fluorescence techniques have attracted immense interest. Synthetic peptide-based fluorescent probes are advantageous over protein-based sensors, since they are synthetically accessible, more stable, and can be easily modified in a site-specific manner for selective biological applications. Peptide receptors labeled with environmentally sensitive/FRET fluorophores have allowed direct detection/monitoring of biomolecules in aqueous media and in live cells. In this review, key peptide-based approaches for different biological applications are presented.

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Arginine mimetic appended peptide-based probes for fluorescence turn-on detection of 14-3-3 proteins

Abstract: Development of fluorescence markers for the 14-3-3 adapter protein class.

Cited by 13 publications

References 25 publications

Multivalent Ligands with Tailor‐Made Anion Binding Motif as Stabilizers of Protein–Protein Interactions

Multivalent Ligands with Tailor‐Made Anion Binding Motif as Stabilizers of Protein–Protein Interactions

Take your Positions and Shine: Effects of Positioning Aggregation‐Induced Emission Luminophores within Sequence‐Defined Macromolecules

Selected peptide-based fluorescent probes for biological applications

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