Linked Life Data

21334412

Source:http://linkedlifedata.com/resource/pubmed/id/21334412

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2011-4-25
pubmed:abstractText
Buforin IIb is a novel cell-penetrating anticancer peptide derived from histone H2A. In this study, we enhanced the cancer targeting specificity of buforin IIb using a tumor-associated enzyme-controlled activation strategy. Buforin IIb was fused with an anionic peptide (modified magainin intervening sequence, MMIS), which neutralizes the positive charge of buforin IIb and thus renders it inactive, via a matrix metalloproteinases (MMPs)-cleavable linker. The resulting MMIS:buforin IIb 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 IIb 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 IIb is enhanced compared to the parent peptide by reactivation at the specialized areas where MMPs are pathologically produced.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1873-5169
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
895-9
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Enhancement of the cancer targeting specificity of buforin IIb by fusion with an anionic peptide via a matrix metalloproteinases-cleavable linker.
pubmed:affiliation
Department of Biology, Research Institute of Life Science, Gyeongsang National University, 900 Gajwa-dong, Jinju 660-701, Republic of Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't