Expert opinion on investigational drugs · 2011
Identification of heptapeptides interacting with IFN-α-sensitive CML cells.
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Liu Jia, Chen Han-chun, Rao Zhou-zhou, Khan Md Asaduzzaman, Wan Xin-xing, Xu Ai-hua, Zhang Nuo, Zhang Dian-zheng
Аннотация
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.
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.
Предметные рубрики MeSH
Angiogenesis InhibitorsBase SequenceCell Line, TumorEnzyme-Linked Immunosorbent AssayEscherichia coliHumansInterferon-alphaLeukemia, Myelogenous, Chronic, BCR-ABL PositiveMolecular Targeted TherapyPeptide LibraryPeptidesPolyethylene GlycolsProtein BindingRecombinant ProteinsSequence Analysis, DNASurvival RateTreatment OutcomeTumor Cells, CulturedUbiquitin-Protein Ligases