Abstract
The present paper describes chain-length effects on helix-forming tendency in sequential peptides containing Z-dehydrophenylalanine (ΔZPhe) residues, i.e., (X-ΔZPhe)n. For sequential peptides Boc-(L-Leu-ΔZPhe)n-L-Leu-OMe (n=2–6) that take 310-helical conformation in CHCl3, solvent dependence on their helical structures was investigated by CD spectroscopy. CD patterns corresponding to a right-handed helix were observed for peptides n=3–6 in CHCl3, tetrahydrofuran, acetonitrile, methanol, and trimethyl phosphate. Such helical structures became less stable in dimethyl sulfoxide and trifluoroethanol. Conformational energy calculation was carried out for acetyl-(L-Ala-ΔZPhe)n-NHCH3 (n=1–12). Peptides above n=2 were predicted to form helical structures preferentially. In addition, rigidity of the helical structure containing ΔZPhe residues was found to be somewhat lower than that containing α-aminoisobutyric acid residue with strong helix-forming tendency. This can be ascribed to the conformational properties inherent in ΔZPhe residue that induces not only helical backbones, but β-turn backbones. Thus, ΔZPhe residue will be useful to design functional peptides having such backbones.
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References
K. Noda, Y. Shimohigashi, and N. Izumiya, “The Peptides,” Vol. 5, E. Gross and J. Meienhofer, Ed., Academic Press, New York, N.Y., 1983, pp 286–339.
E. Gross and J. L. Morell, J. Am. Chem. Soc., 89, 2791 (1967).
H. Allgaier, G. Jung, R. G. Werner, U. Schneider, and H. Zaehner, Eur. J. Biochem., 160, 9 (1986).
I. L. Givot, T. A. Smit, and R. H. Abeles, J. Biol. Chem., 244, 6341 (1969).
R. B. Wickner, J. Biol. Chem., 244, 6550 (1969).
K. R. Rajashankar, S. Ramakumar, and V. S. Chauhan, J. Am. Chem. Soc., 114, 9225 (1992).
O. Pieroni, A. Fissi, C. Pratesi, P. A. Temussi, and F. Ciardelli, J. Am. Chem. Soc., 113, 6338 (1991).
M. R. Ciajolo, A. Tuzi, C. R. Pratesi, A. Fissi, and O. Pieroni, Biopolymers, 30, 911 (1990).
K. K. Bhandary and V. S. Chauhan, Biopolymers, 33, 209 (1993).
B. Padmanbhan and T. P. Singh, Biopolymers, 33, 613 (1993).
V. S. Chauhan, K. Uma, P. Kaur, and P. Balaram, Biopolymers, 28, 763 (1989).
M. R. Ciajoro, A. Tuzi, C. R. Pratesi, A. Fissi, and O. Pieroni, Biopolymers, 32, 717 (1992).
A. Gupta, A. Bharadwaj, and V. S. Chauhan, J. Chem. Soc., Perkin Trans. 2, 1911 (1990).
A. Tuzi, M. R. Ciajolo, G. Guarino, P. A. Temussi, A. Fissi, and O. Pieroni, Biopolymers, 33, 1111 (1993).
O. Pieroni, A. Fissi, C. Pratesi, P. A. Temussi, and F. Ciardelli, Biopolymers, 33, 1 (1993).
M. Iqbal and P. Balaram, Biochemistry, 20, 4866 (1981).
Y. Inai, K. Hasegawa, T. Hirabayashi, and K. Yokota, Polym. J., 28, 238 (1996).
K. Uma and P. Balaram, Indian J. Chem., 28B, 705 (1989), and references therein.
B. V. V. Prasad and P. Balaram, CRC Crit. Rev. Biochem., 16, 307 (1984).
F. Momany, R. F. McGuire, A. W. Burgess, and H. A. Scheraga, J. Phys. Chem., 79, 2361 (1975).
Y. Inai, T. Ito, T. Hirabayashi, and K. Yokota, Biopolymers, 33, 1173 (1993).
Y. Inai, T. Ito, T. Hirabayashi, and K. Yokota, Polym. J., 27, 846 (1995).
M. Sisido, private communications.
Y. Beppu, Comput. Chem., 13, 101 (1989).
M. Oka, Y. Baba, A. Kagemoto, and A. Nakajima, Polym. J., 26, 135 (1990).
M. Oka and A. Nakajima, Polym. Bull., 30, 647 (1993).
S. S. Zimmerman, M. S. Pottle, G. Nemethy, and H. A. Scheraga, Macromolecules, 10, 1 (1975).
N. Harada, S. L. Chen, and K. Nakanishi, J. Am. Chem. Soc., 97, 5345 (1975).
E. K. S. Vijayakumar and P. Balaram, Biopolymers, 22, 2133 (1983).
E. K. S. Viayakumar and P. Balaram, Tetrahedron, 39, 2725 (1983).
I. L. Karle, J. L. Flippen-Anderson, K. Uma, H. Balaram, and P. Balaram, Proc. Natl. Acad. Sci. U.S.A., 86, 765 (1989).
S. Arnott and A. J. Wonacott, J. Mol. Biol., 21, 371 (1966).
Y. Paterson, S. M. Rumsey, E. Benedetti, G. Nemethy, and H. A. Scheraga, J. Am. Chem. Soc., 103, 2947 (1981).
G. N. Ramachandran and V. Sasisekharan, Adv. Protein Chem., 23, 283 (1968).
E. Benedetti, D. B. Benedetto, V. Pavone, C. Pedone, A. Santini, A. Bavoso, C. Toniolo, M. Crisma, and L. Sartore, J. Chem. Soc., Perkin Trans. 2, 1829 (1990).
V. Pavone, E. Benedetti, B. DiBlasio, C. Pedone, A. Santini, A. Bavoso, C. Toniolo, M. Crisma, and L. Sartore, J. Biomol. Struct. Dynam., 7, 1321 (1990).
K. Otoda, Y. Kitagawa, S. Kimira, and Y. Imanishi, Biopolymers, 33, 1337 (1993).
G. Basu and A. Kuki, Biopolymers, 32, 61 (1992).
E. E. Hodgkin, J. D. Clark, K. R. Miller, and G. R. Marshall, Biopolymers, 30, 533 (1990).
J. A. Schellman and C. Schellman, Protein, 2, 1 (1964).
S. Arnott and S. D. Dover, J. Mol. Biol., 30, 209 (1967).
V. S. Chauhan, A. K. Sharma, K. Uma, P. K. C. Paul, and P. Balaram, Int. J. Peptide Proten Res., 29, 126 (1987).
M. Oka and A. Nakajima, Polym. Bull., 33, 693 (1994).
M. Oka, Y. Baba, A. Kagemoto, and A. Nakajima, Polym. J., 22, 185 (1990).
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Inai, Y., Hasegawa, K., Hirabayashi, T. et al. Chain-Length Effects on Helix-Forming Tendency in Sequential Peptides Containing Z-Dehydrophenylalanine Residues. Polym J 28, 440–445 (1996). https://doi.org/10.1295/polymj.28.440
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DOI: https://doi.org/10.1295/polymj.28.440
