Self-aggregation propensity of the Tat peptide revealed by UV-Vis, NMR and MD analyses. Issue 35 (24th August 2017)

• Record Type: Journal Article
• Authors: Macchi, Sara; Nifosì, Riccardo; Signore, Giovanni; Di Pietro, Sebastiano; Boccardi, Claudia; D'Autilia, Francesca; Beltram, Fabio; Cardarelli, Francesco
• Is Part Of: Physical chemistry chemical physics. Volume 19:Issue 35(2017)
• Page Start: 23910
• Page End: 23914
• Publication Date: 2017-08-24
• Subjects: Chemistry, Physical and theoretical -- Periodicals; 541.3
• DOI: 10.1039/c7cp04320a
• Languages: English
• ISSNs: 1463-9076

Abstract

Abstract : The self-aggregation propensity of unlabeled and TAMRA-labeled Tat11 peptides has been revealed for the first time by UV-Vis, NMR and MD analyses. Abstract : By a combination of UV-Vis analyses, NMR-based diffusion measurements and MD simulations we have demonstrated for the first time that the HIV-1 Tat arginine-rich peptide (Tat11 ) is able to self-aggregate in both its fluorescently labeled and unlabeled variants. We propose Tat11 dimerization as the dominant aggregation process and show that the associated equilibrium constant increases ten-fold by labeling with the standard TAMRA dye. Also, we extend similar conclusions to other cationic cell penetrating peptides (CPPs), such as Antennapedia (Ant) and nona-arginine (R9).