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A novel approach for the identification of unique tumor vasculature binding peptides using an E. coli peptide display library.

Identifieur interne : 000076 ( Ncbi/Curation ); précédent : 000075; suivant : 000077

A novel approach for the identification of unique tumor vasculature binding peptides using an E. coli peptide display library.

Auteurs : C K Brown [États-Unis] ; R A Modzelewski ; C S Johnson ; M K Wong

Source :

RBID : pubmed:11129422

Descripteurs français

English descriptors

Abstract

Tumor neovascularization is necessary for continued tumor growth and metastasis. During the process of endothelial cell (EC) recruitment and tumor infiltration, specific molecular markers unique for this interaction are expressed on the EC surface. Targeting these molecular markers would, in effect, allow for specific tumor targeting. Tripeptide sequence motifs have previously been reported that will bind to angiogenic tumor ECs. These sequences were identified from in vivo phage peptide display libraries. The purpose of this study was to use a more simplified bacterial peptide display library in an in vitro system to seek out peptide motifs with unique binding to tumor microvasculature.

DOI: 10.1007/s10434-000-0743-0
PubMed: 11129422

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pubmed:11129422

Le document en format XML

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<term>Endothelium (metabolism)</term>
<term>Escherichia coli</term>
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<term>Neoplasms (blood supply)</term>
<term>Neoplasms (metabolism)</term>
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<term>Neovascularization, Pathologic (metabolism)</term>
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<div type="abstract" xml:lang="en">Tumor neovascularization is necessary for continued tumor growth and metastasis. During the process of endothelial cell (EC) recruitment and tumor infiltration, specific molecular markers unique for this interaction are expressed on the EC surface. Targeting these molecular markers would, in effect, allow for specific tumor targeting. Tripeptide sequence motifs have previously been reported that will bind to angiogenic tumor ECs. These sequences were identified from in vivo phage peptide display libraries. The purpose of this study was to use a more simplified bacterial peptide display library in an in vitro system to seek out peptide motifs with unique binding to tumor microvasculature.</div>
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