Research Article
Spectroscopic Investigations of Pentobarbital Interaction with Transthyretin
Table 2
Percentages of secondary structure components in the amide I and amide II regions of TTR and its pentobarbital complexes.
| Bands | TTR free | TTR + pento 0.12 mM | TTR + pento 0.48 mM | TTR + pento 0.96 mM |
| Amide I | | | | | Parallel β-sheet (1621–1640 cm−1) | 51.6 | 31.3 | 16.9 | 14.7 | Random Coil (1640–1652 cm−1) | 1.7 | 3.4 | 4.2 | 4.0 | α-helix (1652–1666 cm−1) | 6.3 | 8.3 | 7.8 | 8.9 | β-turns (1666–1685 cm−1) | 21.3 | 33.4 | 36.6 | 33.9 | Antiparallel β-sheets (1600–1621 cm−1) (1685–1700 cm−1) | 8.9 10.1 | 13.4 10.3 | 16.0 18.5 | 20.2 18.3 |
| Amide II | | | | | Parallel β-sheet (1490–1507 cm−1) | 45.0 | 27.6 | 6.4 | 5.2 | Antiparallel β-sheet (1507–1528 cm−1) | 0.14 | 12.1 | 35.2 | 32.6 | α-helix (1528–1550 cm−1) | 23.2 | 18.9 | 17.4 | 18.9 | β-turns (1550–1570 cm−1) | 25.3 | 25.5 | 21.6 | 20.17 | Antiparallel β-sheets (1570–1590 cm−1) | 6.3 | 15.9 | 19.3 | 23.2 |
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