A N-alpha-blocked, Aib-rich octapeptide methylamide containing two N-omega-benzoylated L-Lys residues at positions 3 and 6 was synthesized by solution methods and fully characterized. A solution and crystal-state conformational analysis, performed by using FT-IR, H-1 NMR, CD, and X-ray diffraction techniques, showed that the peptide is folded into a regular, right-handed 3(10)-helix stabilized by seven consecutive N-H...O=C intramolecular H-bonds of the beta-tum Ill type. The two benzamidobutyl L-Lys side chains, located on the same side of the helix after one complete turn, generate a cleft the minimal width of which was found to be 3.47 Angstrom.
The Polypeptide 3(10)-helix As A Template For Molecular Recognition Studies - Structural Characterization of A Side-chain Functionalized Octapeptide
TONIOLO, CLAUDIO;FORMAGGIO, FERNANDO;
1995
Abstract
A N-alpha-blocked, Aib-rich octapeptide methylamide containing two N-omega-benzoylated L-Lys residues at positions 3 and 6 was synthesized by solution methods and fully characterized. A solution and crystal-state conformational analysis, performed by using FT-IR, H-1 NMR, CD, and X-ray diffraction techniques, showed that the peptide is folded into a regular, right-handed 3(10)-helix stabilized by seven consecutive N-H...O=C intramolecular H-bonds of the beta-tum Ill type. The two benzamidobutyl L-Lys side chains, located on the same side of the helix after one complete turn, generate a cleft the minimal width of which was found to be 3.47 Angstrom.
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