Abstract
BACKGROUND: Interferon-alpha (IFN-α) is the traditional therapeutic agent for chronic myeloid leukemia (CML). The molecular mechanism of IFN-α efficacy in the treatment of CML is not fully clear.
OBJECTIVES: To identify the peptides and/or proteins that bind to the proteins specifically expressed on the surface of IFN-α-sensitive CML cells by using a phage display library.
DESIGN/METHODS: IFN-α-sensitive KT-1/A3 cells were used as the target, and IFN-α-resistant subline KT-1/A3R was used as absorber for phage display biopanning. The positive phage clones were identified by enzyme-linked immunosorbent assay and flow cytometry. The peptides were deduced from their DNA sequences.
RESULTS: Multiple clones showed high binding efficiency to KT-1/A3 cells compared with that of the other leukemia cells. One of the peptides, KLWVIPQ, has a partial amino acid sequence homology with the C-terminal domain of E3 ubiquitin-protein ligase.
CONCLUSIONS: This study presents the identification of specific heptapeptides that bind to IFN-α-sensitive KT-1/A3 cells. The cancer-selective ligands provide novel strategies for early and differential diagnoses, as well as potential targeted drug delivery.
| Original language | American English |
|---|---|
| Journal | Expert Opinion on Investigational Drugs |
| Volume | 20 |
| State | Published - Dec 1 2011 |
Keywords
- Angiogenesis Inhibitors
- BCR-ABL Positive
- Base Sequence
- Cell Line
- Chronic
- Cultured
- DNA
- Enzyme-Linked Immunosorbent Assay
- Escherichia coli
- Humans
- Interferon-alpha
- Leukemia
- Molecular Targeted Therapy
- Myelogenous
- Peptide Library
- Peptides
- Polyethylene Glycols
- Protein Binding
- Recombinant Proteins
- Sequence Analysis
- Survival Rate
- Treatment Outcome
- Tumor
- Tumor Cells
- Ubiquitin-Protein Ligases
Disciplines
- Medical Immunology
- Medicine and Health Sciences