Enhancement of the cancer targeting specificity of buforin lib by fusion with an anionic peptide via a matrix metalloproteinases-cleavable linker

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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. (C) 2011 Elsevier Inc. All rights reserved.
Publisher
ELSEVIER SCIENCE INC
Issue Date
2011-05
Language
English
Article Type
Article
Keywords

ANTIMICROBIAL PEPTIDE; AMPHIPHILIC PEPTIDES; ANTITUMOR EFFICACY; IV COLLAGENASES; TUMOR-CELLS; EXPRESSION; MATRIX-METALLOPROTEINASE-2; ADENOCARCINOMA; PROGRESSION; CONJUGATE

Citation

PEPTIDES, v.32, no.5, pp.895 - 899

ISSN
0196-9781
URI
http://hdl.handle.net/10203/97413
Appears in Collection
BS-Journal Papers(저널논문)
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