ArticlePloS one2015
TAT Modification of Alpha-Helical Anticancer Peptides to Improve Specificity and Efficacy.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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
29 citing papers in PubMed, 54 citations in OpenAlex.
- Peptide-Drug Conjugates as Next-Generation Therapeutics: Exploring the Potential and Clinical Progress.Bioengineering (Basel, Switzerland) · 2025Review
- Exploring the potential of anticancer peptides as therapeutic agents for cancer treatment.Research in pharmaceutical sciences · 2025Review
- The interplay of carbon and nitrogen cycling driven by watershed microorganisms.Frontiers in microbiology · 2025Review
- A Review of Antibacterial Candidates with New Modes of Action.ACS infectious diseases · 2024Review
- Biological Activity of Natural and Synthetic Peptides as Anticancer Agents.International journal of molecular sciences · 2024Review
- Peptide-Based Agents for Cancer Treatment: Current Applications and Future Directions.International journal of molecular sciences · 2023Review
- Antibiotics in the clinical pipeline as of December 2022.The Journal of antibiotics · 2023Review
- Designed Multifunctional Peptides for Intracellular Targets.Antibiotics (Basel, Switzerland) · 2022Review
- Antimicrobial Peptides and Cationic Nanoparticles: A Broad-Spectrum Weapon to Fight Multi-Drug Resistance Not Only in Bacteria.International journal of molecular sciences · 2022Review
- Computational study, synthesis and evaluation of active peptides derived from Parasporin-2 and spike protein from Alphacoronavirus against colorectal cancer cells.Bioscience reports · 2021Article
- Anticancer activity of Helicobacter pylori ribosomal protein (HPRP) with iRGD in treatment of colon cancer.Journal of cancer research and clinical oncology · 2021Article
- Antimicrobial peptides: mechanism of action, activity and clinical potential.Military Medical Research · 2021Review
- CancerGram: An Effective Classifier for Differentiating Anticancer from Antimicrobial Peptides.Pharmaceutics · 2020Article
- Peptides with Dual Antimicrobial-Anticancer Activity: Strategies to Overcome Peptide Limitations and Rational Design of Anticancer Peptides.Molecules (Basel, Switzerland) · 2020Review
- Anti-cancer peptides: classification, mechanism of action, reconstruction and modification.Open biology · 2020Review
- Antimicrobial Peptides as Anticancer Agents: Functional Properties and Biological Activities.Molecules (Basel, Switzerland) · 2020Review
- Precision medicine by designer interference peptides: applications in oncology and molecular therapeutics.Oncogene · 2020Review
- Review
- Antimicrobial Peptides: Potential Application in Liver Cancer.Frontiers in microbiology · 2019Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
HPRP-A1 is an amphipathic α-helical anticancer peptide (ACP) derived from the N-terminus of ribosomal protein L1 (RpL1) of Helicobacter pylori. In our previously study, HPRP-A1 has been reported that induced HeLa cell apoptosis in a caspase-dependent approach and involved both by the death receptor 'extrinsic' pathway and the mitochondria 'intrinsic' pathway. Here we report the construction of a new hybrid peptide, HPRP-A1-TAT, comprising the cell-permeating peptide TAT linked to the C-terminus of HPRP-A1. This peptide exhibits higher anticancer activity against HeLa cells with lower toxicity against human RBC than HPRP-A1. Two FITC-labeled peptides, FITC-HPRP-A1 and FITC-HPRP-A1-TAT, were used to investigate and compare the cellular uptake mechanism using fluorescence spectra and flow cytometry. Compared with HPRP-A1, HPRP-A1-TAT quickly crossed cell, entered the cytoplasm via endocytosis, and disrupted the cell membrane integrity. HPRP-A1-TAT exhibited stronger anticancer activity than HPRP-A1 at the same concentration by increasing early apoptosis of HeLa cells and inducing caspase activity. Notably, after 24 h, the cellular concentration of HPRP-A1-TAT was higher than that of HPRP-A1. This result suggests that TAT protects HPRP-A1 against degradation, likely due to its high number of positively charged amino acids or the further release of peptides into cancer cells from endocytotic vesicles. We believe that this TAT modification approach may provide an effective new strategy for improving the therapeutic index and anticancer activity of ACPs for clinical use.
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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.