Effect of lengthening of peptide backbone by insertion of chiral β-homo amino acid residues: Conformational behavior of linear peptides containing alternating L-leucine and β-homoL-leucine residues
✍ Scribed by F. Rossi; E. Bucci; C. Isernia; M. Saviano; R. Iacovino; A. Romanelli; P. Di Lello; M. Grimaldi; D. Montesarchio; L. De Napoli; G. Piccialli; E. Benedetti
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2000
- Tongue
- English
- Weight
- 199 KB
- Volume
- 53
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
✦ Synopsis
The synthesis and the solution behavior of the linear peptides containing a -homo (-H) leucine residue-Boc-Leu--HLeu-Leu-OMe, Boc--HLeu-Leu--HLeu-Leu-OMe, and Boc-Leu--HLeu-Leu--HLeu-Leu-OMe-as well as the solid structure of the tripeptide, are reported. The conformational behavior of the peptides was investigated in solution by twodimensional nmr. Our data support the existence in solution with different families of conformers in rapid interchange. The crystals of the tripeptide are orthorhombic, space group P2 1 2 1 2, with a ϭ 15.829(1) Å, b ϭ 29.659(1) Å, c ϭ 6.563(1) Å, and Z ϭ 4. The structure has been solved by direct methods and refined to final R1 and wR2 indexes of 0.0530 and 0.1436 for 2420 reflections with I Ͼ 2(I). In the solid state, the tripeptide does not present intramolecular H bonds, and the