Table 1.
The Ala-scan analogs of Tat1 diversely affect the ChT-L peptidase of the 20S proteasome.
Fig 1.
Inhibitory activity of the peptides with “pharmacophore” regions modified by the Tic-Oic moiety.
Fig 2.
The second derivative of FTIR spectra of Tat1, recorded in H2O, D2O and in a film mode.
Fig 3.
Normalized CD spectra of Tat1 analogs in which the pharmacophore residues were substituted by either Ala or Tic-Oic moiety.
Fig 4.
Overlaid fragments of TOCSY (green-blue) and ROESY (red-yellow) spectra of Tat1_8-9TO (A) and Tat1_8-9TOD (B).
Fig 5.
Chemical shift variation plot between Hα resonances of major conformations of Tat1, Tat1_4-5TO, Tat1_8-9TO, Tat1_8-9TOD, Tat1_4,5TO,8-9TOD and Tat1_A4-5,8–9.
Fig 6.
Superposed conformations obtained in the last 800 ps of MD simulations and surface electrostatic potential maps.
The maps indicate regions of negative potential in red, positive potential in blue, and neutral potential in white. The figures were generated by the MOLMOL). (A) Tat1 [36], (B) Tat1_4-5TO, (C) Tat1_8-9TO, (D) Tat1_8-9TOD, (E) Tat1_4-5TO,8-9TOD and (F) Tat1_A4-5,8–9. RMSD values are 0.800, 1.008, 1.357, 1.187, 0.865 and 1.140 Å for the backbone atoms in the fragment 1–9 of Tat1, Tat1_4-5TO, Tat1_8-9TO, Tat1_8-9TOD, Tat1_4-5TO,8-9TOD and Tat1_A4-5,8–9, respectively.
Table 2.
Statistics of distance and dihedral angle restraints used for 3D structure calculations and quality ensemble of 200 NMR-derived structures of the peptides on the last steps of MD simulations with the time-averaged distance and dihedral angle restraints.