ArticlePharmaceutics2021
PL1 Peptide Engages Acidic Surfaces on Tumor-Associated Fibronectin and Tenascin Isoforms to Trigger Cellular Uptake.
Article in Pharmaceutics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Multistage nanomedicine engineering to overcome sequential barriers to glioblastoma treatment: a review.Journal of nanobiotechnology · 2026Review
- A Review of Current Computational Tools for Peptide-Protein Docking.Journal of computational chemistry · 2026Review
- Magnetic Detection of Cancer Cells Using Tumor-Homing Peptide-Modified Magnetic Nanoparticles.Biosensors · 2026Article
- Serum-MiR-CanPred: deep learning framework for pan-cancer classification and miRNA-targeted drug discovery.RNA biology · 2025Article
- Targeting oncofetal fibronectin and neuropilin-1 in solid tumors with PL2 peptide.Scientific reports · 2025Article
- Advances and prospects of cell-penetrating peptides in tumor immunotherapy.Scientific reports · 2025Review
- Emerging Approaches in Glioblastoma Treatment: Modulating the Extracellular Matrix Through Nanotechnology.Pharmaceutics · 2025Review
- In Vitro Study of Tumor-Homing Peptide-Modified Magnetic Nanoparticles for Magnetic Hyperthermia.Molecules (Basel, Switzerland) · 2024Article
- The role of TNC in atherosclerosis and drug development opportunities.International journal of biological sciences · 2024Review
- Editorial on Special Issue "Precision Delivery of Drugs and Imaging Agents with Peptides".Pharmaceutics · 2022Article
- Homing Peptide-Based Targeting of Tenascin-C and Fibronectin in Endometriosis.Nanomaterials (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tumor extracellular matrix (ECM) is a high-capacity target for the precision delivery of affinity ligand-guided drugs and imaging agents. Recently, we developed a PL1 peptide (sequence: PPRRGLIKLKTS) for systemic targeting of malignant ECM. Here, we map the dynamics of PL1 binding to its receptors Fibronectin Extra Domain B (FN-EDB) and Tenascin C C-isoform (TNC-C) by computational modeling and cell-free binding studies on mutated receptor proteins, and study cellular binding and internalization of PL1 nanoparticles in cultured cells. Molecular dynamics simulation and docking analysis suggested that the engagement of PL1 peptide with both receptors is primarily driven by electrostatic interactions. Substituting acidic amino acid residues with neutral amino acids at predicted PL1 binding sites in FN-EDB (D52N-D49N-D12N) and TNC-C (D39N-D45N) resulted in the loss of binding of PL1 nanoparticles. Remarkably, PL1-functionalized nanoparticles (NPs) were not only deposited on the target ECM but bound the cells and initiated a robust cellular uptake via a pathway resembling macropinocytosis. Our studies establish the mode of engagement of the PL1 peptide with its receptors and suggest applications for intracellular delivery of nanoscale payloads. The outcomes of this work can be used for the development of PL1-derived peptides with improved stability, affinity, and specificity for precision targeting of the tumor ECM and malignant cells.
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