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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2010.1
- 수록면
- 561 - 566 (6page)
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Though protein transduction domains (PTDs) are well known for the delivery of exogenous therapeutic proteins into living cells, the overall low efficiency of transduction is a serious obstacle. We investigated the effect of bog blueberry anthocyanins (BBA) on protein transduction efficiency and found that BBA enhanced the transduction efficiencies of Tat-SOD fusion protein into HeLa cells and mice skin. The enzymatic activities in the cells and skin tissue in the presence of BBA were markedly increased compared to controls. Further, BBA did not demonstrate any cell toxicity at various concentrations. Although the mechanism is not fully understood, we suggest that BBA might alter the conformation of the membrane, which would indicate that BBA can be used as a protein transduction enhancer for the efficient delivery of therapeutic proteins for a variety of disorders.
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참고문헌 (24)
참고문헌 신청
[학술지
An, J. J. / 2008 / Transduced human PEP-1-heat shock protein 27 efficiently protects against brain ischemic insult / FEBS J. 275 : 1296 ~ 1308
Bannister, J. V. / 1987 / Assays for superoxide dismutase / Methods Biochem. Anal. 32 : 279 ~ 312
Choi, S. H. / 2006 / Human PEP-1-ribosomal protein S3 protects against UV-induced skin cell death / FEBS Lett. 580 : 6755 ~ 6762
Dietz, G. P. / 2010 / Cell-penetrating peptide technology to delivery chaperones and associated factors in diseases and basic research / Curr. Pharm. Biotechnol. 11 : 167 ~ 1
An, J. J. / 2008 / Transduced human PEP-1-heat shock protein 27 efficiently protects against brain ischemic insult / FEBS J. 275 : 1296 ~ 1308
Bannister, J. V. / 1987 / Assays for superoxide dismutase / Methods Biochem. Anal. 32 : 279 ~ 312
Choi, S. H. / 2006 / Human PEP-1-ribosomal protein S3 protects against UV-induced skin cell death / FEBS Lett. 580 : 6755 ~ 6762
Dietz, G. P. / 2010 / Cell-penetrating peptide technology to delivery chaperones and associated factors in diseases and basic research / Curr. Pharm. Biotechnol. 11 : 167 ~ 1
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