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A New Peptidic Vector for Molecular Imaging of Apoptosis, Identified by Phage Display Technology
1 Department of General, Organic and Biomedical Chemistry, NMR and Molecular Imaging Laboratory, University of Mons-Hainaut, Mons, Belgium.
* To whom correspondence should be addressed. E-mail: robert.muller{at}umh.ac.be.
Phosphatidylserine (PS) exposure on the cell surface is an early marker of apoptosis. To select PS binding peptides as vectors of contrast agents to image apoptosis, a phage library has been exposed to perfused mouse livers. Phages not retained on control livers during the first perfusions were used for selections on apoptotic livers in a second series of perfusions. Four selected phages were further evaluated for binding to PS-coated enzyme-linked immunosorbent assay (ELISA) plates. They presented an apparent affinity constant (Ka app) for PS ranging from 6.08 x 1010 M to 1.62 x 1011 M. These phages did not bind to phosphatidylcholine, and competition with annexin V confirmed their specific interaction with PS. The phage with the highest affinity-bound PS in ELISA with a Ka app = (1.6 ± 0.2) x 1011 M. It carried the TLVSSL peptide that was synthesized. Specific competition with annexin V and with the synthetic peptide was performed and confirms the specificity of the interaction. Key Words: phage display, apoptosis, phosphatidylserine, MRI, contrast agent
First published on June 7, 2006, doi:10.1177/1087057106288220 This article has been cited by other articles:
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