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Issue 35, 2017
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Self-aggregation propensity of the Tat peptide revealed by UV-Vis, NMR and MD analyses

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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).

Graphical abstract: Self-aggregation propensity of the Tat peptide revealed by UV-Vis, NMR and MD analyses

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Publication details

The article was received on 27 Jun 2017, accepted on 14 Aug 2017 and first published on 14 Aug 2017


Article type: Communication
DOI: 10.1039/C7CP04320A
Citation: Phys. Chem. Chem. Phys., 2017,19, 23910-23914
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    Self-aggregation propensity of the Tat peptide revealed by UV-Vis, NMR and MD analyses

    S. Macchi, R. Nifosì, G. Signore, S. Di Pietro, C. Boccardi, F. D'Autilia, F. Beltram and F. Cardarelli, Phys. Chem. Chem. Phys., 2017, 19, 23910
    DOI: 10.1039/C7CP04320A

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