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

BMB Reports

Tae-Hyung Lee^1¹ 

[1] Department of Biochemistry and Molecular Biology, Yeungnam University College of Medicine, Daegu 705-717, Korea^1

关键词: Methionine sulfoxide reductase;   

DOI  :  

学科分类：生物化学/生物物理

来源: Korean Society for Biochemistry and Molecular Biology

【 摘 要 】

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.

【 授权许可】

Unknown