Istituto di Biofisica     
Tuzi A., Ciajolo M. R., Picone D., Crescenzi O., Temussi P. A., Fissi A., Pieroni O. 3-10-Helices, Helix Screw Sense and Screw Sense Reversal in the Dehydro-peptide Boc-Val-Phe-Gly-Phe-Val-OMe. In: Journal of Peptide Science, vol. 2 (1) pp. 47 - 58. Wiley, 1996.
The pentapeptide Boc-Val-Phe-Gly-Phe-Val-OMe, containing two dehydro-phenylalanine (Phe) residues, has been synthesized and its structure investigated. In the crystalline state, the molecule adopts a right-handed 310-helical conformation stabilized by two intramolecular hydrogen bonds between CO of Val1 and NH of Phe4, and between CO of Phe2 and NH of Val5, respectively. NMR measurements are consistent with the presence of 310-helical structures also in acetonitrile and dimethylsulphoxide solution: the distances between backbone protons estimated from NOE connectivities are in overall agreement with those observed in the solid state; the chemical shifts of the amide protons show the smaller temperature coefficients for the NHs that in solid state are involved in intramolecular hydrogen bonds. The CD spectra in acetonitrile, chloroform, methanol and dimethylsulphoxide display exciton couplets of bands corresponding to the Phe electronic transition at 280nm; the sign of the bands is consistent with the presence of helical structures having a prevalent left-handed screw sense. Addition of 1,1,1,3,3,3-hexafluoro- propan-2-ol gives rise to the gradual appearance of a couplet of opposite sign, suggesting the helix reversal from left-handed sense to right-handed sense. The conformational behaviour is discussed on the basis of the specific sequence of the peptide.
URL: http://www3.interscience.wiley.com/journal/24504/abstract
Subject Dehydro-peptides 310-helix
Helix reversal
Crystal structure
Circular dichroism

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