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Identification of Heptapeptides Interacting with IFN-α-Sensitive CML cells
Expert Opinion on Investigational Drugs
  • Jia Liu, Department of Biochemistry, School of Biological Science and Technology , Central South University, Changsha, 410013, Hunan, China
  • Hanchun Chen, Department of Biochemistry, School of Biological Science and Technology , Central South University, Changsha, 410013, Hunan, China
  • Zhou-zhou Rao, Department of Gynecology and Obstetrics , the Second Xiangya Hospital of Central South University, Changsha, Hunan 410011, China
  • Md. Asaduzzaman Khan, Department of Biochemistry, School of Biological Science and Technology , Central South University, Changsha, 410013, Hunan, China
  • Xin-Xing Wan, Department of Biochemistry, School of Biological Science and Technology , Central South University, Changsha, 410013, Hunan, China
  • Ai-hua Xu, Department of Biochemistry, School of Biological Science and Technology , Central South University, Changsha, 410013, Hunan, China
  • Nuo Zhang, Department of Biochemistry, School of Biological Science and Technology , Central South University, Changsha, 410013, Hunan, China
  • Dianzheng Zhang, Philadelphia College of Osteopathic Medicine
Document Type
Article
Publication Date
12-1-2011
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.
PubMed ID
22092230
Comments

This article was published in Expert Opinion on Investigational Drugs, Volume 20, Issue 12, December 2011, pages 1583-1589.

The published version is available at http://dx.doi.org/10.1517/13543784.2011.632407

Copyright © 2011 Informa Plc.

Citation Information
Jia Liu, Hanchun Chen, Zhou-zhou Rao, Md. Asaduzzaman Khan, et al.. "Identification of Heptapeptides Interacting with IFN-α-Sensitive CML cells" Expert Opinion on Investigational Drugs Vol. 20 Iss. 12 (2011) p. 1583 - 1589
Available at: http://works.bepress.com/dianzheng_zhang/11/