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2006-01-01 - Article/Dans un journal avec peer-review - Anglais - 9 page(s)

Laumonier C., Segers J., Laurent Sophie , Michel A., Coppée Frédérique , Belayew Alexandra , Vander Elst Luce , Muller Robert , "A new peptidic vector for molecular imaging of apoptosis, identified by phage display technology" in Journal of Biomolecular Screening : The Official Journal of the Society for Biomolecular Screening, 11, 5, 537-545

  • Edition : SAGE Publications, Thousand Oaks (CA)
  • Codes CREF : Biochimie (DI3112), Biologie moléculaire (DI3111)
  • Unités de recherche UMONS : Chimie générale, organique et biomédicale (M108), Biologie moléculaire (M122)
Texte intégral :

Abstract(s) :

(Anglais) 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 10(10) M to 1.62 x 10(11) 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 10(11) 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.

Identifiants :
  • PMID : 16760366
  • ISSN : 1087-0571
  • DOI : 10.1177/1087057106288220