ArticleACS chemical biology2020
Engineering Cell-Permeable Proteins through Insertion of Cell-Penetrating Motifs into Surface Loops.
Article in ACS chemical biology, 2020. 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, 21 citations in OpenAlex.
- Protein Modifications for Cellular Protein Delivery.Chemical reviews · 2026Review
- Intracellular Delivery of Peptides and Proteins with an Engineered Membrane Translocation Domain.ACS chemical biology · 2026Article
- Intracellular Delivery of Peptides and Proteins with an Engineered Membrane Translocation Domain.bioRxiv : the preprint server for biology · 2026Article
- Selection of Nucleotide-Encoded Mass Libraries of Macrocyclic Peptides for Inaccessible Drug Targets.Chemical reviews · 2024Review
- Evaluation of the Cytosolic Uptake of HaloTag Using a pH-Sensitive Dye.ACS chemical biology · 2024Article
- Targeting the ExpandedACS omega · 2023Article
- The endosomal escape vehicle platform enhances delivery of oligonucleotides in preclinical models of neuromuscular disorders.Molecular therapy. Nucleic acids · 2023Article
- How Do Biomolecules Cross the Cell Membrane?Accounts of chemical research · 2022Article
- Cell-Penetrating Peptides.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Effective delivery of proteins into the cytosol of mammalian cells would open the door to a wide range of applications. However, despite great efforts from numerous investigators, effective protein delivery in a clinical setting is yet to be accomplished. Herein we report a potentially general approach to engineering cell-permeable proteins by genetically grafting a short cell-penetrating peptide (CPP) to an exposed loop of a protein of interest. The grafted peptide is conformationally constrained, exhibiting enhanced proteolytic stability and cellular entry efficiency. Applying this technique to enhanced green fluorescent protein (EGFP), protein-tyrosine phosphatase 1B (PTP1B), and purine nucleoside phosphorylase (PNP) rendered all three proteins cell-permeable and biologically active in cellular assays. When added into growth medium at 0.5-5 μM concentrations, the engineered PTP1B dose-dependently reduced the phosphotyrosine levels of intracellular proteins, while the modified PNP corrected the metabolic deficiency of PNP-deficient mouse T lymphocytes, providing a potential enzyme replacement therapy for a rare genetic disease.
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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.