Self-association of a highly charged arginine-rich cell-penetrating peptide - Université Grenoble Alpes
Article Dans Une Revue Proceedings of the National Academy of Sciences of the United States of America Année : 2017

Self-association of a highly charged arginine-rich cell-penetrating peptide

Résumé

Significance Arginine-rich cell-penetrating peptides are promising candidates for intracellular drug delivery. These cationic peptides spontaneously traverse biological membranes via a direct mode of entry which is not yet fully understood. In this study, we report the complex solution behavior of the cell-penetrating peptide deca-arginine. Despite its large net positive charge, deca-arginine self-associates at low-to-intermediate ionic strengths, owing to an interaction mode which is present in the structure of a significant number of proteins. Self-association may thus enhance the bioavailability of deca-arginine. Our findings provide the key to the understanding of the self-association mechanism in deca-arginine with implications for the potential biological roles of this unusual binding motif.

Dates et versions

hal-04537156 , version 1 (08-04-2024)

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Citer

Giulio Tesei, Mario Vazdar, Malene Ringkjøbing Jensen, Carolina Cragnell, Phil Mason, et al.. Self-association of a highly charged arginine-rich cell-penetrating peptide. Proceedings of the National Academy of Sciences of the United States of America, 2017, 114 (43), pp.11428-11433. ⟨10.1073/pnas.1712078114⟩. ⟨hal-04537156⟩
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