Solid-state conformations of aminosuccinyl peptides: Crystal structure of tert-butyloxycarbonyl-L-leucyl-L-aminosuccinyl-L-phenylalaninamide

✍ Scribed by S. Capasso; L. Mazzarella; F. Sica; A. Zagari

• Book ID: 102762412
• Publisher: Wiley (John Wiley & Sons)
• Year: 1989
• Tongue: English
• Weight: 501 KB
• Volume: 28
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.360280116

✦ Synopsis

The protected tripeptide ter6butyloxycarbonyl-L-leucyl-L-~~uccinyl-L-phenylalan~~de crystalliz? in the orthorhombic space group p2,2,2,, with a = 6.214(3), b = 12.832(3), c = 33.094(4) A, Z = 4. The structure was solved by direct methods using MULTAN 80 and refined to an R value of 0.055 for 1458 reflections. The bond lengths and angles are in good agreement with the standard values. The peptide backbone adopts a type 11' B-bend conformation with a weak intramolecular hydrogen bond between the CO group of the leucyl residue and the C-terminal NH, group. In agreement with previous studies, this structure confirms the high propensity of aminosuccinyl peptides to adopt a type 11' 8-bend conformation. The role of this conformation in relation to the deamidation process in proteins is also discussed.

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