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

Self-aggregation propensity of the Tat peptide revealed by UV-Vis, NMR and MD analyses.
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Macchi S, Nifosì R, Signore G, Di Pietro S, Boccardi C, D'Autilia F, Beltram F, Cardarelli F,


Macchi S, Nifosì R, Signore G, Di Pietro S, Boccardi C, D'Autilia F, Beltram F, Cardarelli F, (click to view)

Macchi S, Nifosì R, Signore G, Di Pietro S, Boccardi C, D'Autilia F, Beltram F, Cardarelli F,

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Physical chemistry chemical physics : PCCP 19(35) 23910-23914 doi 10.1039/c7cp04320a

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).

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