Fig. 5: Titrations of 15N HSQC of 2N4R 15N-Tau (20 μM) with β-Tau and β-Hsp90 in buffer solution (50 mM NaPi pH 6.8, 10 mM NaCl, 1 mM DTT, 10% D2O) at 5 °C (900 MHz or 800 MHz) at a mole ratio of Wt-Tau441/compounds = 1/5. | Nature Communications

Fig. 5: Titrations of 15N HSQC of 2N4R 15N-Tau (20 μM) with β-Tau and β-Hsp90 in buffer solution (50 mM NaPi pH 6.8, 10 mM NaCl, 1 mM DTT, 10% D2O) at 5 °C (900 MHz or 800 MHz) at a mole ratio of Wt-Tau441/compounds = 1/5.

From: Synthetic chaperone based on Hsp90-Tau interaction inhibits Tau aggregation and rescues physiological Tau-Microtubule interaction

Fig. 5

Indicated in orange circles (A) and (B) are the locations of selected hydrophobic amino acids (F, Y, I, L, V, P) in the sequence of Wt-Tau. A Chemical shift perturbations (CSP) of Tau residues in the presence of β-Hsp90 (red) are more prominent than those of β-Tau (violet), particularly in the P1 region of Tau (residues ~175-187, within the region boxed in gray). Black triangles represent noise-level CSP values (B) I/I0 values of Tau residues (I represents NMR signal intensity in the presence of peptide, and I0 corresponds to conditions in the absence of compounds) showed a ~ 20% decrease upon addition of β-Hsp90 at the 1/5 mole ratio (also in Supplementary Fig. 8), however this was not observed for the same mole ratio upon addition of β-Tau.

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