Abstract
In sequential peptides Boc-(L-Leu-ΔPhe)n-L-Leu-OMe I-n, n=2–6 (Boc, t-butoxycarbonyl; OMe, methoxy), peptides above n=2 were already found to form a stable right-handed 310-helical structure in solution. In the present study, we focused on whether the above chain-length dependence on helical stability retains in the solid state, or not. For this purpose, FT-IR and CD spectra were measured for peptides I-n in the solid state and in solution. In FT-IR spectra of peptides I-3 to I-6 in KBr and in chloroform, two major peaks were observed in amide I absorption band: i.e., first peak at 1665–1655 cm−1 assigned to Leu residues in helical segments, and second peak at 1628–1625 cm−1 assigned to ΔPhe residues in helical segments. FT-IR pattern of peptide I-2 differed from those of peptides I-3 to I-6 in the solid state and in solution essentially. CD spectra of peptides I-n in KBr appeared clearly and strongly. Except for peptide I-2, peptides I-3 to I-6 in the solid state showed exciton couplets with a negative peak at longer wavelengths around 280 nm (assignable to ΔPhe residues), similarly to those in chloroform. The sign of split CD pattern corresponds to a right-handed arrangement of the transition moment: i.e., ΔPhe residues are arranged regularly along a right-handed helical main chain. As a result, a stable helix is formed in the peptides above n=2 in the solid state as well as in solution.
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Inai, Y., Sakakura, Y. & Hirabayashi, T. FT-IR and CD Measurement of Z-Dehydrophenylalanine-Containing Peptides in the Solid State and in Solution. Polym J 30, 828–832 (1998). https://doi.org/10.1295/polymj.30.828
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DOI: https://doi.org/10.1295/polymj.30.828