title: Identification of heptapeptides interacting with IFN-α-sensitive CML cells.
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.
  
  
  OBJECTIVE
  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.
  
  
  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.
authors.affiliation: Department of Biochemistry, School of Biological Science and Technology, Central South University, Changsha, 410013, Hunan, China.
authors.forename: Jia
authors.initials: J
authors.lastname: Liu
authors.forename: Han-chun
authors.initials: HC
authors.lastname: Chen
authors.forename: Zhou-zhou
authors.initials: ZZ
authors.lastname: Rao
authors.forename: Md Asaduzzaman
authors.initials: MA
authors.lastname: Khan
authors.forename: Xin-xing
authors.initials: XX
authors.lastname: Wan
authors.forename: Ai-hua
authors.initials: AH
authors.lastname: Xu
authors.forename: Nuo
authors.initials: N
authors.lastname: Zhang
authors.forename: Dian-zheng
authors.initials: DZ
authors.lastname: Zhang
mesh_terms: D020533:Angiogenesis Inhibitors / Q000378:metabolism / Q000627:therapeutic use; D001483:Base Sequence; D045744:Cell Line, Tumor; D004797:Enzyme-Linked Immunosorbent Assay; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism; D006801:Humans; D016898:Interferon-alpha / Q000378:metabolism / Q000494:pharmacology* / Q000627:therapeutic use; D015464:Leukemia, Myelogenous, Chronic, BCR-ABL Positive / Q000188:drug therapy* / Q000378:metabolism; D058990:Molecular Targeted Therapy; D019151:Peptide Library; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D011092:Polyethylene Glycols / Q000378:metabolism / Q000627:therapeutic use*; D011485:Protein Binding; D011994:Recombinant Proteins / Q000378:metabolism / Q000627:therapeutic use; D017422:Sequence Analysis, DNA; D015996:Survival Rate; D016896:Treatment Outcome; D014407:Tumor Cells, Cultured; D044767:Ubiquitin-Protein Ligases / Q000737:chemistry* / Q000378:metabolism
chemical_list: D020533:Angiogenesis Inhibitors; D016898:Interferon-alpha; D019151:Peptide Library; D010455:Peptides; D011994:Recombinant Proteins; D011092:Polyethylene Glycols; D044767:Ubiquitin-Protein Ligases; C100416:peginterferon alfa-2a