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Advances and prospects of cell-penetrating peptides in tumor immunotherapy
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“Likewise, tumor-penetrating peptides (e.g., iRGD/CendR pathway) have been broadly used as penetration-promoting modules in peptide-drug conjugates and nanocarriers; when combined with cleavable linkers (e.g., reducible/disulfide or enzyme-responsive motifs), they can improve intratumoral dispersion while helping limit off-target exposure [89].”
From Overcoming tumor microenvironment barriers: transformable and bioinspired nanomedicine strategies for deep tumor penetration (2026) · cites this paper as [89]
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Endosomal escape pathways for delivery of biologicals
Varkouhi, A. K., Scholte, M., Storm, G., & Haisma, H. J. (2011) · Journal of Controlled Release · doi:10.1016/j.jconrel.2010.11.004 · Cited by 1,561
Kim, H., Seo, E.-H., Lee, S.-H., & Kim, B.-J. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17122054 · Cited by 48
Research works printed but not linked: 101
- Papaioannou, N. E. et al. Harnessing the immune system to improve cancer therapy. Ann. Transl. Med. 4(14), 261–261 (2016). · DOI
- Cha, J.-H. et al. New approaches on cancer immunotherapy. Cold Spring Harbor Perspect. Med. 10(8), a036863 (2020). · DOI
- Galon, J. & Bruni, D. Approaches to treat immune hot, altered and cold tumours with combination immunotherapies. Nat. Rev. Drug Discovery 18(3), 197–218 (2019). · DOI
- Frankel, A.D. and Pabo, C.O. Cellular uptake of the tat protein from human immunodeficiency virus. Cell55(6), 1189–1193 (1988). · DOI
- Bottens, R. A. & Yamada, T. Cell-penetrating peptides (CPPs) as therapeutic and diagnostic agents for cancer. Cancers 14(22), 5546 (2022). · DOI
- Sun, Z. et al. Cell-penetrating peptide-based delivery of macromolecular drugs: development, strategies, and progress. Biomedicines 11(7), 1971 (2023). · DOI
- Tripathi, P.P., et al., Cell penetrating peptides in preclinical and clinical cancer diagnosis and therapy. Oncotarget 9(98), 37252–37267 (2018). · DOI
- Jankovic, J. et al. Injectable daxibotulinumtoxina in cervical dystonia: A phase 2 dose-escalation multicenter study. Mov. Disord. Clin. Pract. 5(3), 273–282 (2018). · DOI
- Meyer-Losic, F. et al. DTS-108, a novel peptidic prodrug of SN38: In vivo efficacy and toxicokinetic studies. Clin. Cancer Res. 14(7), 2145–2153 (2008). · DOI
- Lingasamy, P. et al. Bi-specific tenascin-C and fibronectin targeted peptide for solid tumor delivery. Biomaterials 219, 119373 (2019). · DOI
- Ding, N., et al. iRGD synergizes with PD-1 knockout immunotherapy by enhancing lymphocyte infiltration in gastric cancer. Nat. Commun. 10(1) 2019. · DOI
- Hasannejad-Asl, B. et al. Cell penetrating peptide: A potent delivery system in vaccine development. Front. Pharmacol. 13, 1072685 (2022). · DOI · Paper page
- Xie, J. et al. Cell-penetrating peptides in diagnosis and treatment of human diseases: From preclinical research to clinical application. Front. Pharmacol. 11, 697 (2020). · DOI
- Yin, H. et al., iRGD as a tumor-penetrating peptide for cancer therapy. Molecular Medicine Reports 15(5),2925–2930 (2017). · DOI
- Tian, Y. et al. A doxorubicin delivery platform using engineered natural membrane vesicle exosomes for targeted tumor therapy. Biomaterials 35(7), 2383–2390 (2014). · DOI
- Lingasamy, P., Laarmann, A.-H. & Teesalu, T. Tumor penetrating peptide-functionalized tenascin-C antibody for glioblastoma targeting. Curr. Cancer Drug Targets 21(1), 70–79 (2021). · DOI
- Liu, C. et al. iRGD-mediated core-shell nanoparticles loading carmustine and O6-benzylguanine for glioma therapy. J. Drug Target. 25(3), 235–246 (2016). · DOI
- Ponnappan, N. & Chugh, A. Cell-penetrating and cargo-delivery ability of a spider toxin-derived peptide in mammalian cells. Eur. J. Pharm. Biopharm. 114, 145–153 (2017). · DOI
- Taylor, B. N. et al. Noncationic peptides obtained from azurin preferentially enter cancer cells. Cancer Res. 69(2), 537–546 (2009). · DOI
- Yamada, T., Das Gupta, T. K. & Beattie, C. W. p28, an anionic cell-penetrating peptide, increases the activity of wild type and mutated p53 without altering its conformation. Mol. Pharm. 10(9), 3375–3383 (2013). · DOI
- Silva, S. et al. A second life for MAP, a model amphipathic peptide. Int. J. Mol. Sci. 23(15), 8322 (2022). · DOI
- Lingasamy, P. et al. PL1 peptide engages acidic surfaces on tumor-associated fibronectin and tenascin isoforms to trigger cellular uptake. Pharmaceutics 13(12), 1998 (2021). · DOI
- Taylor, B.N., et al., Noncationic Peptides Obtained From Azurin Preferentially Enter Cancer Cells. Cancer Research. 69(2), 537–546 (2009). · DOI
- Dietz, G.P.H., Cell-Penetrating Peptide Technology to Deliver Chaperones and Associated Factors in Diseases an Basic Research. Current Pharmaceutical Biotechnology 11(2), 167–174 (2010). · DOI
- Burlina, F. et al. Quantification of the cellular uptake of cell-penetrating peptides by MALDI-TOF mass spectrometry. Angew. Chem. Int. Ed. 44(27), 4244–4247 (2005). · DOI
- Futaki, S. & Nakase, I. Cell-surface interactions on arginine-rich cell-penetrating peptides allow for multiplex modes of internalization. Acc. Chem. Res. 50(10), 2449–2456 (2017). · DOI
- Madani, F. et al. Mechanisms of cellular uptake of cell-penetrating peptides. J. Biophys. 2011, 1–10 (2011). · DOI
- Erazo-Oliveras, A. et al. Improving the endosomal escape of cell-penetrating peptides and their cargos: Strategies and challenges. Pharmaceuticals 5(11), 1177–1209 (2012). · DOI
- El-Sayed, A., Futaki, S. & Harashima, H. Delivery of macromolecules using arginine-rich cell-penetrating peptides: Ways to overcome endosomal entrapment. AAPS J. 11(1), 13–22 (2009). · DOI
- El-Andaloussi, S. et al. Induction of splice correction by cell-penetrating peptide nucleic acids. J. Gene Med. 8(10), 1262–1273 (2006). · DOI
- cationic cell penetrating peptides as source ther deliv 2015 apr 6 4 491 507.pdf. · DOI
- Veldhoen, S. et al. Cellular delivery of small interfering RNA by a non-covalently attached cell-penetrating peptide: quantitative analysis of uptake and biological effect. Nucleic Acids Res. 34(22), 6561–6573 (2006). · DOI
- Fretz, M. M. et al. Temperature-, concentration- and cholesterol-dependent translocation of L- and D-octa-arginine across the plasma and nuclear membrane of CD34+ leukaemia cells. Biochem. J. 403(2), 335–342 (2007). · DOI
- Lulla, R. R. et al. Phase I trial of p28 (NSC745104), a non-HDM2-mediated peptide inhibitor of p53 ubiquitination in pediatric patients with recurrent or progressive central nervous system tumors: A pediatric brain tumor consortium study. Neuro-Oncology 18(9), 1319–1325 (2016). · DOI
- Freeman-Keller, M. & Weber, J. S. Anti-programmed death receptor 1 immunotherapy in melanoma: Rationale, evidence and clinical potential. Ther. Adv. Med. Oncol. 7(1), 12–21 (2014). · DOI
- Nixon, B. G. & Li, M. O. Satb1: Restraining PD1 and T Cell Exhaustion. Immunity 46(1), 3–5 (2017). · DOI
- Wang, J. et al. Fibrinogen-like protein 1 is a major immune inhibitory ligand of LAG-3. Cell 176(1–2), 334-347.e12 (2019). · DOI
- Wan, W.-J. et al. Coadministration of iRGD peptide with ROS-sensitive nanoparticles co-delivering siFGL1 and siPD-L1 enhanced tumor immunotherapy. Acta Biomater. 136, 473–484 (2021). · DOI
- Zhang, M. et al. Recombinant cell-penetrating trichosanthin synergizes anti-PD-1 therapy in colorectal tumor. Int. J. Biol. Sci. 19(6), 1698–1712 (2023). · DOI
- Zhou, S. et al. Bifunctional iRGD-anti-CD3 enhances antitumor potency of T cells by facilitating tumor infiltration and T-cell activation. J. ImmunoTher. Cancer 9(5), e001925 (2021). · DOI
- Zhu, M. et al. Combination therapy with iRGD-antiCD3 and PD-1 blockade enhances antitumor potency of cord blood-Derived T Cells. OncoTargets Ther. 14, 835–844 (2021). · DOI
- Zhang, W. et al. A bispecific peptide-polymer conjugate bridging target-effector cells to enhance immunotherapy. Adv. Healthc. Mater. 12(18), 2202977 (2023). · DOI
- Yang, D. S. et al. A redox-triggered bispecific supramolecular nanomedicine based on peptide self-assembly for high-efficacy and low-toxic cancer therapy. Adv. Funct. Mater. 30(4), 1904969 (2019). · DOI
- Dal Corso, A. et al. A non-internalizing antibody-drug conjugate based on an anthracycline payload displays potent therapeutic activity in vivo. J. Control. Release 264, 211–218 (2017). · DOI · Paper page
- Munn, D.H., et al., Inhibition of T cell proliferation by macrophage tryptophan catabolism. J. Experimental Medicine. 189(9), 1363–1372 (1999). · DOI
- Li, G. et al. Dual-blockade immune checkpoint for breast cancer treatment based on a tumor-penetrating peptide assembling nanoparticle. ACS Appl. Mater. Interfaces 11(43), 39513–39524 (2019). · DOI
- Chen, Y. et al. Prodrug-like, PEGylated protein toxin trichosanthin for reversal of chemoresistance. Mol. Pharm. 14(5), 1429–1438 (2017). · DOI
- Met, Ö. et al. Principles of adoptive T cell therapy in cancer. Semin. Immunopathol. 41(1), 49–58 (2018). · DOI
- Dong, Y. et al. iRGD-modified memory-like NK cells exhibit potent responses to hepatocellular carcinoma. J. Transl. Med. 21(1), 205 (2023). · DOI
- Cogdill, A. P. et al. Targeting the MAGE A3 antigen in pancreatic cancer. Surgery 152(3), S13–S18 (2012). · DOI
- Derouazi, M. et al. Novel cell-penetrating peptide-based vaccine induces robust CD4+ and CD8+ T cell-mediated antitumor immunity. Cancer Res. 75(15), 3020–3031 (2015). · DOI
- Lim, S., Koo, J.-H. & Choi, J.-M. Use of cell-penetrating peptides in dendritic cell-based vaccination. Immune Netw. 16(1), 33 (2016). · DOI
- Pouniotis, D. et al. Vaccine delivery by penetratin: Mechanism of antigen presentation by dendritic cells. Immunol. Res. 64(4), 887–900 (2016). · DOI
- Backlund, C.M., et al., Cell-penetrating peptides enhance peptide vaccine accumulation and persistence in lymph nodes to drive immunogenicity. Proceedings of the National Academy of Sciences of the United States of America. 119(32) (2022). · DOI · Paper page
- Fu, X. et al. Staphylococcal enterotoxin C2 mutant drives T lymphocyte activation through PI3K/mTOR and NF-ĸB signaling pathways. Toxicol. Appl. Pharmacol. 333, 51–59 (2017). · DOI
- Song, Y. et al. An iRGD peptide fused superantigen mutant induced tumor-targeting and T lymphocyte infiltrating in cancer immunotherapy. Int. J. Pharm. 586, 119498 (2020). · DOI
- Wu, H. et al. Cell-penetrating peptide enhanced antigen presentation for cancer immunotherapy. Bioconjugate Chem. 30(8), 2115–2126 (2019). · DOI
- Pouniotis, D. S. et al. Whole protein and defined CD8+ and CD4+ peptides linked to penetratin targets both MHC class I and II antigen presentation pathways. Immunol. Cell Biol. 89(8), 904–913 (2011). · DOI
- Brooks, N. et al. Immunogenicity of a tripartite cell penetrating peptide containing a MUC1 variable number of tandem repeat (VNTR) and a T helper epitope. Molecules 23(9), 2233 (2018). · DOI
- Jiang, J. Cell-penetrating peptide-mediated nanovaccine delivery. Curr. Drug Targets 22(8), 896–912 (2021). · DOI
- Liu, X. et al. A cell-penetrating peptide-assisted nanovaccine promotes antigen cross-presentation and anti-tumor immune response. Biomater. Sci. 7(12), 5516–5527 (2019). · DOI
- Tang, J. et al. A novel self-assembled nanoparticle vaccine with HIV-1 Tat49-57/HPV16 E749–57 fusion peptide and GM-CSF DNA elicits potent and prolonged CD8+ T cell-dependent anti-tumor immunity in mice. Vaccine 30(6), 1071–1082 (2012). · DOI
- Staff, C. et al. Telomerase (GV1001) vaccination together with gemcitabine in advanced pancreatic cancer patients. Int. J. Oncol. 45(3), 1293–1303 (2014). · DOI
- Lee, S.-A. et al. Heat shock protein-mediated cell penetration and cytosolic delivery of macromolecules by a telomerase-derived peptide vaccine. Biomaterials 34(30), 7495–7505 (2013). · DOI
- Yang, J. et al. Cell-penetrating Peptides: Efficient vectors for vaccine delivery. Curr. Drug Deliv. 16(5), 430–443 (2019). · DOI
- Zhou, M. et al. The role of cell-penetrating peptides in potential anti-cancer therapy. Clin. Transl. Med. 12(5), e822 (2022). · DOI
- Wang, K. et al. Cell penetrating peptide-based redox-sensitive vaccine delivery system for subcutaneous vaccination. Mol. Pharm. 15(3), 975–984 (2018). · DOI
- Zhang, T. T. et al. LAH4 enhances CD8+ T cell immunity of protein/peptide-based vaccines. Vaccine 30(4), 784–793 (2012). · DOI
- Saleh, T. et al. MPG-based nanoparticle: An efficient delivery system for enhancing the potency of DNA vaccine expressing HPV16E7. Vaccine 33(28), 3164–3170 (2015). · DOI
- Granadillo, M. et al. LALF32-51-E7 therapeutic vaccine induces antitumor immunity against human papillomavirus type 16 E7-expressing murine tumor metastases in the lungs. Clin. Exp. Metastasis 34(3–4), 241–249 (2017). · DOI
- Fisher, P. B. Is mda-7/IL-24 a “Magic Bullet” for Cancer?. Cancer Res. 65(22), 10128–10138 (2005). · DOI
- Menezes, M. E. et al. MDA-7/IL-24: Multifunctional Cancer Killing Cytokine. In Anticancer Genes (ed. Grimm, S.) 127–153 (Springer London, London, 2014). · DOI
- Singh, A. P. et al. IL-24 inhibits lung cancer cell migration and invasion by disrupting the SDF-1/CXCR4 signaling axis. Plos One 10(3), e0122439 (2015). · DOI
- Yang, J. et al. Modification of IL-24 by tumor penetrating peptide iRGD enhanced its antitumor efficacy against non-small cell lung cancer. Int. Immunopharmacol. 70, 125–134 (2019). · DOI
- Dharanipragada, R., New modalities in conformationally constrained peptides for potency, selectivity and cell permeation. Future Medicinal Chemistry. 5(7), 831–849 (2013). · DOI
- Koppelhus, U., et al., Improved cellular activity of antisense peptide nucleic acids by conjugation to a cationic peptide-lipid (CatLip) domain. Bioconjugate Chemistry. 19(8), 1526–1534 (2008). · DOI
- Shi, N.-Q. et al. A survey on “Trojan Horse” peptides: Opportunities, issues and controlled entry to “Troy”. J. Control. Release 194, 53–70 (2014). · DOI
- Derakhshankhah, H. & Jafari, S. Cell penetrating peptides: A concise review with emphasis on biomedical applications. Biomed. Pharmacother. 108, 1090–1096 (2018). · DOI
- Zakeri-Milani, P., et al., Cytotoxicity and Immunogenicity Evaluation of Synthetic Cell-penetrating Peptides for Methotrexate Delivery. Iran J Pharm Res. 20(3), 506–515 (2021).
- Palm, C. et al. Peptide degradation is a critical determinant for cell-penetrating peptide uptake. Biochim. Biophys. Acta 1768(7), 1769–1776 (2007). · DOI
- Ruoslahti, E. Tumor penetrating peptides for improved drug delivery. Adv. Drug Deliv. Rev. 110–111, 3–12 (2017). · DOI
- Gustafson, H. H. et al. Nanoparticle uptake: The phagocyte problem. Nano Today 10(4), 487–510 (2015). · DOI
- Patel, A., K. Cholkar, and A.K. Mitra, Recent developments in protein and peptide parenteral delivery approaches. Therapeutic delivery. 5(3), 337–65 (2014). · DOI
- Di, L. Strategic approaches to optimizing peptide ADME properties. AAPS J. 17(1), 134–143 (2014). · DOI · Paper page
- Lee, J. S. & Tung, C.-H. Lipo-oligoarginines as effective delivery vectors to promote cellular uptake. Mol. BioSyst. 6(10), 2049 (2010). · DOI
- Lu, J. et al. D- and unnatural amino acid substituted antimicrobial peptides with improved proteolytic resistance and their proteolytic degradation characteristics. Front. Microbiol. 11, 563030 (2020). · DOI
- Nischan, N. et al. Stabilization of peptides for intracellular applications by phosphoramidate-linked polyethylene glycol chains. Angew. Chem. Int. Ed. 52(45), 11920–11924 (2013). · DOI
- the polyethyleneglycol dilemma adva source biol pharm bull so 2013 36 6 892 9.pdf. · DOI
- Kumar, S. et al. PEGylation and cell-penetrating peptides: Glimpse into the past and prospects in the future. Curr. Topics Med. Chem. 20(5), 337–348 (2020). · DOI
- Qian, Z. et al. Intracellular delivery of peptidyl ligands by reversible cyclization: Discovery of a PDZ domain inhibitor that rescues CFTR activity. Angew. Chem. Int. Ed. 54(20), 5874–5878 (2015). · DOI
- Qian, Z. et al. Discovery and mechanism of highly efficient cyclic cell-penetrating peptides. Biochem. 55(18), 2601–2612 (2016). · DOI
- Lättig-Tünnemann, G. et al. Backbone rigidity and static presentation of guanidinium groups increases cellular uptake of arginine-rich cell-penetrating peptides. Nat. Commun. 2(1), 453 (2011). · DOI
- Guarracino, D. A. et al. Macrocyclic control in helix mimetics. Chem. Rev. 119(17), 9915–9949 (2019). · DOI
- Nieberler, M. et al. Exploring the role of RGD-recognizing integrins in cancer. Cancers 9(12), 116 (2017). · DOI
- Zhu, L. et al. Research progress of radiolabeled asn-gly-arg (NGR) peptides for imaging and therapy. Mol. Imaging 19, 1536012120934957 (2020). · DOI
- Säälik, P. et al. Peptide-guided nanoparticles for glioblastoma targeting. J. Control. Release 308, 109–118 (2019). · DOI
- de Jong, H., Bonger, K. M. & Löwik, D. W. P. M. Activatable cell-penetrating peptides: 15 years of research. RSC Chem. Biol. 1(4), 192–203 (2020). · DOI
- Schach, D. K. et al. Reversible activation of a cell-penetrating peptide in a membrane environment. J. Am. Chem. Soc. 137(38), 12199–12202 (2015). · DOI
- Futaki, S., et al., Stearylated arginine-rich peptides: A new class of transfection systems. Bioconjugate Chemistry. 12(6), 1005–1011 (2001). · DOI
- Pham, W. et al. Enhancing membrane permeability by fatty acylation of oligoarginine peptides. ChemBioChem 5(8), 1148–1151 (2004). · DOI
- Lingasamy, P. et al. Tumor-penetrating peptide for systemic targeting of tenascin-C. Sci. Rep. 10(1), 5809 (2020). · DOI
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Sheng, J., Yuan, W., Zhang, M., Chen, Z., Qi, Y., Zhao, Y., & Zhang, S. (2026) · Journal of Nanobiotechnology · doi:10.1186/s12951-026-04028-7 · Cited by 35
Metadata
- Authors
- Yang, D., Liu, B., & Sha, H.
- Venue
- Scientific Reports
- Published
- 2025-01-27
- Volume
- 15
- Issue
- 1
- ISSN
- 2045-2322
- PMC
- PMC11772771
- Cited by
- 31
- References
- 2
- Language
- en
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