ArticleThe Analyst2013
β-Turn sequences promote stability of peptide substrates for kinases within the cytosolic environment.
Article in The Analyst, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 14 citations in OpenAlex.
- Cross-Species Applications of Peptide Substrate Reporters to Quantitative Measurements of Kinase Activity.ACS measurement science au · 2024Article
- CPProtectides: Rapid uptake of well-folded β-hairpin peptides with enhanced resistance to intracellular degradation.Peptide science (Hoboken, N.J.) · 2019Article
- Assays for tyrosine phosphorylation in human cells.Methods in enzymology · 2019Article
- Design and Application of Sensors for Chemical Cytometry.ACS chemical biology · 2018Review
- N-Gemini peptides: cytosolic protease resistance via N-terminal dimerization of unstructured peptides.Chemical communications (Cambridge, England) · 2017Article
- Targeting kinase signaling pathways with constrained peptide scaffolds.Pharmacology & therapeutics · 2017Review
- Development of β-Hairpin Peptides for the Measurement of SCF-Family E3 Ligase Activity in Vitro via Ornithine Ubiquitination.ACS omega · 2017Article
- Identification of a p53-based portable degron based on the MDM2-p53 binding region.The Analyst · 2016Article
- Separation of peptide fragments of a protein kinase C substrate fused to a β-hairpin by capillary electrophoresis.Analytical and bioanalytical chemistry · 2015Article
- Pronase E-Based Generation of Fluorescent Peptide Fragments: Tracking Intracellular Peptide Fate in Single Cells.Analytical chemistry · 2015Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
A strategy was developed to extend the lifetime of an peptide-based substrate for Abl kinase in the cytosolic environment. Small β-turn structures were added to the peptide's N-terminus to block entry into peptidase catalytic sites. The influence of the size of the β-turn and two covalent cross-linking strategies on the rate of hydrolysis was assessed. The most peptidase-resistant substrate was degraded at a rate of 0.6 pmol mg(-1) s(-1) and possessed a half-life of 20.3 ± 1.7 min in a Baf/BCR-ABL cytosolic lysate, representing 16- and 40-fold improvements, respectively, over that of a control peptide lacking the β-turn structure. Furthermore, the kcat/KM value of this peptide was 432 μM(-1) min(-1), a 1.25× increase over the unmodified control, verifying that the added β-turn did not hinder the substrate properties of the peptide. This improved peptide was microinjected into single Baf/BCR-ABL cells and substrate phosphorylation measured. Zero to forty percent of the peptide was phosphorylated in the single cells. In contrast, when the control peptide without a β-turn was loaded into cells, the peptide was too rapidly degraded to detect phosphorylation. This work demonstrates that small β-turn structures can render peptides more resistant to hydrolysis while retaining substrate efficacy and shows that these stabilized peptides have the potential to be of high utility in single-cell enzyme assays.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.