DI-UMONS : Dépôt institutionnel de l’université de Mons

Recherche transversale
(titres de publication, de périodique et noms de colloque inclus)
2013-06-30 - Colloque/Présentation - poster - Anglais - 1 page(s)

Henoumont Céline , Place Sarah, Vander Elst Luce , Laurent Sophie , Muller Robert , "Study by the STD NMR technique of the interaction between peptides targeting the αVβ3 integrin and PANC-1 cells" in Euromar, Hersonissos, Grèce (Crète), 2013

  • Codes CREF : Résonance magnétique nucléaire (biophysique) (DI131B)
  • Unités de recherche UMONS : Chimie générale, organique et biomédicale (M108)
  • Instituts UMONS : Institut des Sciences et Technologies de la Santé (Santé), Institut des Biosciences (Biosciences)
  • Centres UMONS : Centre de Recherche en Microscopie et Imagerie Médicale (CMMI)

Abstract(s) :

(Anglais) Molecular Imaging by MRI is a fastly growing field of research. It involves the development of molecular contrast agents with a high affinity for a target molecule which is expressed or overexpressed in pathological conditions. Since several years, our laboratory has chosen the strategy of grafting on MRI contrast agents small peptides with a high affinity for a target molecule. The evaluation of the association constant of the peptide with its target is thus a very important step, and NMR appears to be a very attractive tool. Many interesting target molecules are however membrane-bound proteins, which are often difficult to deal with in solution. They indeed lose their structure and function when they are removed from their natural membrane environment. It is thus important to be able to study the non covalent interactions with these proteins directly on cells. As reported in the literature [1], the STD NMR technique is particularly appropriate. The STD NMR technique consists in the selective irradiation of the protein NMR spectrum, which results in saturation of the protein signals and of any ligand protons interacting with the protein. This is the so-called “on-resonance” spectrum. Subtraction of this spectrum from the one collected with the selective irradiation out of the NMR spectrum of the protein and the ligand (the so-called “off-resonance” spectrum) gives the saturation transfer difference spectrum, in which only protons interacting with the protein are visible. As a proof of concept, we have studied here the non covalent interactions between different peptides containing the RGD sequence known to interact with integrin αVβ3 and PANC-1 cells, which overexpress this integrin. [1] Claasen, B., Axmann, M., Meinecke, R., Meyer, B. J. Am. Chem. Soc. 2005, 127, 916-919.