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- Title
Multimerization of an apoptogenic TRAIL-mimicking peptide by using adamantane-based dendrons.
- Authors
Lamanna, Giuseppe; Smulski, Cristian R; Chekkat, Neila; Estieu-Gionnet, Karine; Guichard, Gilles; Fournel, Sylvie; Bianco, Alberto
- Abstract
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.
- Publication
Chemistry (Weinheim an der Bergstrasse, Germany), 2013, Vol 19, Issue 5, p1762
- ISSN
1521-3765
- Publication type
Journal Article
- DOI
10.1002/chem.201202415