ArticlePloS one2015
Quantitative analysis of ligand-EGFR interactions: a platform for screening targeting molecules.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.
What it found
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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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
24 citing papers in PubMed, 36 citations in OpenAlex.
- Comparative Real-Time Kinetics of Ligand-Receptor Interactions Using Immobilization-Based Sensing Readouts.Analytical chemistry · 2026Article
- From Blood Flow to Tumor Cell Internalization: A Multistage Computational Model of Nanoparticle Dynamics.Pharmaceutical research · 2026Article
- Enhanced Chemical Method for Bispecific Antibody Production: Leveraging Site-Specific Conjugation and Stable Crosslinker Technology.Methods in molecular biology (Clifton, N.J.) · 2026Article
- High-throughput thermodynamic fingerprinting of protein-ligand interactions by DNA-directed focal molography.PloS one · 2026Article
- First-in-Human Study of ABY-029, a Novel Fluorescent Peptide that Targets EGFR, Applied to Soft-Tissue Sarcomas.Molecular cancer therapeutics · 2025Article
- Epidermal growth factor receptor in placental health and disease: pathways, dysfunction, and chemical disruption.Toxicological sciences : an official journal of the Society of Toxicology · 2025Review
- AFM reveals differential effects of acidification on LDL- and oxidized LDL-receptor interactions: biomechanical implications in atherogenesis.Cellular & molecular biology letters · 2025Article
- Fluidic Interface for Surface-based DNA Origami Studies.ACS applied materials & interfaces · 2024Article
- Bispecific Antibodies Produced via Chemical Site-Specific Conjugation Technology: AJICAP Second-Generation.ACS medicinal chemistry letters · 2023Article
- Selecting Nanobodies Specific for the Epidermal Growth Factor from a Synthetic Nanobody Library.Molecules (Basel, Switzerland) · 2023Article
- Cell-Based Sensors for the Detection of EGF and EGF-Stimulated CaBiosensors · 2023Article
- Potential of Epidermal Growth Factor-like Peptide from the Sea CucumberMarine drugs · 2022Article
- Identification of potential targets of the curcumin analog CCA-1.1 for glioblastoma treatment : integrated computational analysis and in vitro study.Scientific reports · 2022Article
- Article
- Biodistribution and Activity of EGFR Targeted Polymeric Micelles Delivering a New Inhibitor of DNA Repair to Orthotopic Colorectal Cancer Xenografts with Metastasis.Molecular pharmaceutics · 2022Article
- EGFR-Binding Peptides: From Computational Design towards Tumor-Targeting of Adeno-Associated Virus Capsids.International journal of molecular sciences · 2020Article
- Mammalian Expression andACS omega · 2020Article
- Prediction of regulatory targets of alternative isoforms of the epidermal growth factor receptor in a glioblastoma cell line.BMC bioinformatics · 2019Article
- Synthesis, Microtubule-Binding Affinity, and Antiproliferative Activity of New Epothilone Analogs and of an EGFR-Targeted Epothilone-Peptide Conjugate.International journal of molecular sciences · 2019Article
- Peptide-nanoparticle conjugates: a next generation of diagnostic and therapeutic platforms?Nano convergence · 2018Review
Corrections and comments
- Erratum issued
Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Epidermal growth factor receptor (EGFR) is often constitutively stimulated in many cancers owing to the binding of ligands such as epidermal growth factor (EGF). Therefore, it is necessary to investigate the interaction between EGFR and its targeting biomolecules. The main aim of this study was to estimate the binding affinity and adhesion force of two targeting molecules, anti-EGFR monoclonal antibody (mAb LA1) and the peptide GE11 (YHWYGYTPQNVI), with respect to EGFR and to compare these values with those obtained for the ligand, EGF. Surface plasmon resonance (SPR) was used to determine the equilibrium dissociation constant (KD) for evaluating the binding affinity. Atomic force microscopy (AFM) was performed to estimate the adhesion force. In the case of EGFR, the KD of EGF, GE11, and mAb LA1 were 1.77 × 10-7, 4.59 × 10-4 and 2.07 × 10-9, respectively, indicating that the binding affinity of mAb LA1 to EGFR was higher than that of EGF, while the binding affinity of GE11 to EGFR was the lowest among the three molecules. The adhesion force between EGFR and mAb LA1 was 210.99 pN, which is higher than that observed for EGF (209.41 pN), while the adhesion force between GE11 and EGFR was the lowest (59.51 pN). These results suggest that mAb LA1 binds to EGFR with higher binding affinity than EGF and GE11. Moreover, the adhesion force between mAb LA1 and EGFR was greater than that observed for EGF and GE11. The SPR and AFM experiments confirmed the interaction between the receptor and targeting molecules. The results of this study might aid the screening of ligands for receptor targeting and drug delivery.
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What OpenQuestion holds
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.