Article Dans Une Revue Chemistry - A European Journal Année : 2012

Multimerization of an Apoptogenic TRAIL-Mimicking Peptide by Using Adamantane-Based Dendrons

Résumé

We have developed a straightforward strategy to multimerize an apoptogenic peptide that mimics the natural tumor necrosis factor‐related apoptosis‐inducing ligand (TRAIL) by using adamantane‐based dendrons as multivalent scaffolds. The selective binding affinity of the ligands to TRAIL receptor 2 (TR2) was studied by surface plasmon resonance, thus demonstrating that the trimeric and hexameric forms of the peptide exert an increased affinity of about 1500‐ and 20 000‐fold, respectively, relative to the monomer. Moreover, only the trimeric and hexameric ligands were able to induce cell death in TR2 expressing cells (BJAB), thus confirming that a multivalent form of the peptide is necessary to trigger a substantial TR2‐dependent apoptotic response in vitro. These results provide interesting insight into the multivalency effect on biological ligand/receptor interactions for future therapeutic applications.

Dates et versions

hal-02557761 , version 1 (28-04-2020)

Identifiants

Citer

Giuseppe Lamanna, Cristian Smulski, Neïla Chekkat, Karine Estieu-Gionnet, Gilles Guichard, et al.. Multimerization of an Apoptogenic TRAIL-Mimicking Peptide by Using Adamantane-Based Dendrons. Chemistry - A European Journal, 2012, 19 (5), pp.1762-1768. ⟨10.1002/chem.201202415⟩. ⟨hal-02557761⟩
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