ArticleAnnals of translational medicine2020
Screening and identification of a CD44v6 specific peptide using improved phage display for gastric cancer targeting.
Article in Annals of translational medicine, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- Phage Display as a Promising Platform for Peptide Drug Discovery.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Peptide-based inhibition of CD44v6 renders liver carcinomas more susceptible to therapeutic intervention.Journal of molecular medicine (Berlin, Germany) · 2025Article
- Review
- Bacteriophage-based strategies for biocontrol and treatment of infectious diseases.Computational and structural biotechnology journal · 2025Review
- Advancements in research leveraging phage display technology for gastric cancer diagnosis and treatment.Frontiers in microbiology · 2025Review
- Review
- Review
- Strategies for the Isolation and Identification of Gastric Cancer Stem Cells.Stem cells international · 2024Review
- Targeting CD44 Variant 5 with an Antibody-Drug Conjugate Is an Effective Therapeutic Strategy for Intrahepatic Cholangiocarcinoma.Cancer research · 2023Article
- Multi-modal imaging for uptake of peptide ligand specific for CD44 by hepatocellular carcinoma.Photoacoustics · 2022Article
- Review
- Mechanisms of Dendrobium officinale polysaccharides in repairing gastric mucosal injuries based on mitogen-activated protein kinases (MAPK) signaling pathway.Bioengineered · 2022Article
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundPeptide probes can be applied for biomarker targeting to improve the diagnostic accuracy. Cluster of differentiation 44 (CD44) is up-regulated in gastric cancer (GC). Among all the variants of CD44, CD44v6 is reported the most promising biomarker for GC. The purpose of this study was generating and identification a peptide ligand specific to CD44v6.
methodsA 12-mer phage peptide library was screened on CD44v overexpressed HEK-293 cells with an improved subtractive method. Five candidate sequences emerged. Candidate phages were selected using enzyme-linked immunosorbent assay and competitive inhibition assays. Then the sequence (designated ELT) was chosen for further study. Its binding affinity and specificity were verified on recombinant protein, GC cells, GC tissues and xenograft models based on BALB/c-nu/nu mice using dissociation constant calculation, immunofluorescence, immunohistochemistry and
resultsThe dissociation constant of ELT with recombinant protein was 611.2 nM. ELT stained CD44v overexpressed HEK-293 but not the cell expressing wild-type CD44s. On GC cell lines, ELT co-stained with anti-CD44v6 antibody. ELT binding on tumor tissues significantly increased compared with that of paracancer tissues, also showed a linear positive correlation with CD44v6 expression. ELT specifically accumulated in tumor and eliminated in short time
conclusionsELT can target GC
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