Identification and characterization of a suite of tumor targeting peptides for non-small cell lung cancer
| Autor: | John V. Heymach, Lixia Diao, Lei Wu, Dorothy Cupka, Kathlynn Brown, Shaghayegh Rezaie, John D. Minna, Ying Horng Liu, Shunzi Li, James Issac, Naveen Pattisapu, Bethany Powell Gray, Lauren Averett Byers, Xian Jin Xie, Michael J. McGuire, Tsukasa Oyama |
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| Rok vydání: | 2014 |
| Předmět: |
Lung Neoplasms
Genotype Peptide Plasma protein binding Biopanning Biology Ligands Article Mice Drug Delivery Systems Peptide Library Carcinoma Non-Small-Cell Lung Cell Line Tumor medicine Animals Cluster Analysis Humans Amino Acid Sequence Peptide library Peptide sequence chemistry.chemical_classification Multidisciplinary Molecular Structure Cell Surface Display Techniques Cancer medicine.disease Molecular biology 3. Good health Disease Models Animal Protein Transport Phenotype chemistry Cell culture Cancer research Heterografts Protein Multimerization Peptides Protein Binding |
| Zdroj: | Scientific Reports |
| ISSN: | 2045-2322 |
| Popis: | Tumor targeting ligands are emerging components in cancer therapies. Widespread use of targeted therapies and molecular imaging is dependent on increasing the number of high affinity, tumor-specific ligands. Towards this goal, we biopanned three phage-displayed peptide libraries on a series of well-defined human non-small cell lung cancer (NSCLC) cell lines, isolating 11 novel peptides. The peptides show distinct binding profiles across 40 NSCLC cell lines and do not bind normal bronchial epithelial cell lines. Binding of specific peptides correlates with onco-genotypes and activation of particular pathways, such as EGFR signaling, suggesting the peptides may serve as surrogate markers. Multimerization of the peptides results in cell binding affinities between 0.0071–40 nM. The peptides home to tumors in vivo and bind to patient tumor samples. This is the first comprehensive biopanning for isolation of high affinity peptidic ligands for a single cancer type and expands the diversity of NSCLC targeting ligands. |
| Databáze: | OpenAIRE |
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