Synthesis and application of fluorescein- and biotin-labeled molecular probes for the chemokine receptor CXCR4.
Publication/Presentation Date
5-5-2008
Abstract
The design, synthesis, and bioevaluation of fluorescence- and biotin-labeled CXCR4 antagonists are described. The modification of D-Lys8 at an epsilon-amino group in the peptide antagonist Ac-TZ14011 derived from polyphemusin II had no significant influence on the potent binding of the peptide to the CXCR4 receptor. The application of the labeled peptides in flow cytometry and confocal microscopy studies demonstrated the selectivity of their binding to the CXCR4 receptor, but not to CXCR7, which was recently reported to be another receptor for stromal cell-derived factor 1 (SDF-1)/CXCL12.
Volume
9
Issue
7
First Page
1154
Last Page
1158
ISSN
1439-7633
Published In/Presented At
Oishi, S., Masuda, R., Evans, B., Ueda, S., Goto, Y., Ohno, H., Hirasawa, A., Tsujimoto, G., Wang, Z., Peiper, S. C., Naito, T., Kodama, E., Matsuoka, M., & Fujii, N. (2008). Synthesis and application of fluorescein- and biotin-labeled molecular probes for the chemokine receptor CXCR4. Chembiochem : a European journal of chemical biology, 9(7), 1154–1158. https://doi.org/10.1002/cbic.200700761
Disciplines
Business Administration, Management, and Operations | Health and Medical Administration | Management Sciences and Quantitative Methods
PubMedID
18412193
Department(s)
Administration and Leadership
Document Type
Article