Identification of Heptapeptides Interacting with IFN-α-Sensitive CML cells

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.

Publication Title

Expert Opinion on Investigational Drugs

Volume

20

Issue

12

First Page

1583

Last Page

1589

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.

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