ArticleACS omega2022
Tuning of Peptide Cytotoxicity with Cell Penetrating Motif Activatable by Matrix Metalloproteinase-2.
Article in ACS omega, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed.
- Polyethylene glycol incorporation to reduce the cytotoxicity associated with cationic cell-penetrating-peptide conjugation.RSC medicinal chemistry · 2025Article
- Anti-breast cancer activity of a novel genetically engineered fusion protein composed of HER2 affibody and proapoptotic peptide R8-KLA.Medical oncology (Northwood, London, England) · 2025Article
- Strike Mitochondria By Enzyme-Instructed Self-Assembled Peptides for Effective Immunogenic Anti-Tumor Therapy.International journal of nanomedicine · 2025Article
- Cell-Penetrating Peptide-Mediated Biomolecule Transportation in Artificial Lipid Vesicles and Living Cells.Molecules (Basel, Switzerland) · 2024Review
- Interaction of KLAKLAK-NHPharmaceutics · 2024Article
- Peptide-Mediated Nanocarriers for Targeted Drug Delivery: Developments and Strategies.Pharmaceutics · 2024Review
- Toxicity Studies of Cardiac-Targeting Peptide Reveal a Robust Safety Profile.Pharmaceutics · 2024Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although diverse cell penetrating motifs not only from naturally occurring proteins but also from synthetic peptides have been discovered and developed, the selectivity of cargo delivery connected to these motifs into the desired target cells is generally low. Here, we demonstrate the selective cytotoxicity tuning of an anticancer KLA peptide with a cell penetrating motif activatable by matrix metalloproteinase-2 (MMP2). The anionic masking sequence introduced at the end of the KLA peptide through an MMP2-cleavable linker is selectively cleaved by MMP2 and the cationic cell penetrating motif is activated. Upon treatment of the peptide to H1299 cells (high MMP2 level), it is selectively internalized into the cells by MMP2, which consequently induces membrane disruption and cell death. In contrast, the peptide shows negligible cytotoxicity toward A549 cancer cells with low MMP2 levels. Furthermore, the selective therapeutic efficacy of the peptide induced by MMP2 is also corroborated using in vivo study.
Identifiers
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Registered trials
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