Enhancement of the cancer targeting specificity of buforin lib by fusion with an anionic peptide via a matrix metalloproteinases-cleavable linker
- Title
- Enhancement of the cancer targeting specificity of buforin lib by fusion with an anionic peptide via a matrix metalloproteinases-cleavable linker
- Author
- 이진원
- Keywords
- Buforin lib; Anticancer peptide; Antimicrobial peptide; Fusion peptide; Matrix metalloproteinase
- Issue Date
- 2011-02
- Publisher
- ELSEVIER SCIENCE INC
- Citation
- PEPTIDES, v. 32, NO 5, Page. 895-899
- Abstract
- Buforin Ilb is a novel cell-penetrating anticancer peptide derived from histone H2A. In this study, we enhanced the cancer targeting specificity of buforin Ilb using a tumor-associated enzyme-controlled activation strategy. Buforin Ilb was fused with an anionic peptide (modified magainin intervening sequence, MMIS), which neutralizes the positive charge of buforin lib and thus renders it inactive, via a matrix metalloproteinases (MMPs)-cleavable linker. The resulting MMIS:buforin Ilb fusion peptide was completely inactive against MMPs-nonproducing cells. However, when the fusion peptide was administrated to MMPs-producing cancer cells, it regained the killing activity by releasing free buforin Ilb through MMPs-mediated cleavage. Moreover, the activity of the fusion peptide toward MMPs-producing cancer cells was significantly decreased when the cells were pretreated with a MMP inhibitor. Taken together, these data indicate that the cancer targeting specificity of MMIS:buforin Ilb is enhanced compared to the parent peptide by reactivation at the specialized areas where MMPs are pathologically produced.
- URI
- https://www.sciencedirect.com/science/article/pii/S0196978111000799
- ISSN
- 0196-9781; 1873-5169
- DOI
- 10.1016/j.peptides.2011.02.010
- Appears in Collections:
- COLLEGE OF NATURAL SCIENCES[S](자연과학대학) > LIFE SCIENCE(생명과학과) > Articles
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