ArticleChemistry (Weinheim an der Bergstrasse, Germany)2021
Modulation of Src Kinase Activity by Selective Substrate Recognition with Pseudopeptidic Cages.
Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Molecular Recognition of Tyrosine-Containing Polypeptides with Pseudopeptidic Cages Unraveled by Fluorescence and NMR Spectroscopies.Bioconjugate chemistry · 2023Article
- Substrate Protection in Controlled Enzymatic Transformation of Peptides and Proteins.Chembiochem : a European journal of chemical biology · 2021Article
- Modulation of Src Kinase Activity by Selective Substrate Recognition with Pseudopeptidic Cages.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
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Authors and funding
6 authors.
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Abstract
The selective recognition of tyrosine residues in peptides is an appealing approach to inhibiting their tyrosine kinase (TK)-mediated phosphorylation. Herein, we describe pseudopeptidic cages that efficiently protect substrates from the action of the Src TK enzyme, precluding the corresponding Tyr phosphorylation. Fluorescence emission titrations show that the most efficient cage inhibitors strongly bind the peptide substrates with a very good correlation between the binding constant and the inhibitory potency. Structural insights and additional control experiments further support the proposed mechanism of selective supramolecular protection of the substrates. Moreover, the approach also works in a completely different kinase-substrate system. These results illustrate the potential of supramolecular complexes for the efficient and selective modulation of TK signaling.
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