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The protein truncation caused by fusion of PEP-1 peptide and protective roles of transduced PEP-1-MsrA in skin cells

  • Lee, Tae-Hyung (Department of Biochemistry and Molecular Biology, Yeungnam University College of Medicine) ;
  • Choi, Seung-Hee (Department of Biochemistry and Molecular Biology, Yeungnam University College of Medicine) ;
  • Kim, Hwa-Young (Department of Biochemistry and Molecular Biology, Yeungnam University College of Medicine)
  • Received : 2010.12.21
  • Accepted : 2011.01.26
  • Published : 2011.04.30

Abstract

PEP-1 peptide has been used for transduction of native protein into mammalian cells. This work describes the findings that the fusion of PEP-1 to target proteins led to protein truncation likely in a non-protein-specific manner. Approximately 75% of PEP-1-MsrA fusion protein was truncated in the N-terminal region of MsrA between Lys-27 and Val-28 during expression in Escherichia coli and purification. This large protein truncation was also observed in another PEP-1 fused protein, PEP-1-MsrB2, in the N-terminal region of MsrB2. The full-length PEP-1-MsrA protein was rapidly transduced into keratinocyte cells within 15 min. The transduced PEP-1-MsrA was functionally active and could protect skin cells against oxidative stress- and ultraviolet radiation-induced cell death. Collectively, our data demonstrated the protective roles of MsrA in skin cells and, moreover, may raise a concern of protein truncation caused by fusion of PEP-1 about the general use of this peptide for protein transduction.

Keywords

References

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