Acta Crystallographica Section B

Structural Science

Volume 54, Part 3 (June 1998)

research papers

Acta Cryst. (1998). B54, 300-307 [ doi:10.1107/S0108768197013402 ]

Structure of Z-(Aib)₉OBu^t

R. Geßmann, H. Brückner and M. Kokkinidis

Abstract: The structure of the synthetic protected oligopeptide Z-(Aib)₉OBu^t, tert-butoxynona( [alpha] -aminoisobutyric acid), which contains the unusual [alpha] -aminoisobutyric acid (Aib), was determined by X-ray crystallography. The two independent molecules in the asymmetric unit fold into 3₁₀-helices, each stabilized by seven intramolecular hydrogen bonds. The C terminus of one of the molecules is disordered and adopts a semi-extended conformation, which is rather unusual for Aib residues. This is the first observation of such a conformation involved in a disorder in Aib-containing oligopeptides. The existence of a second conformation for the C-terminal residue might explain the difficulties in crystallizing the title compound and a different behaviour of the title compound in thin layer chromatography compared with the other homopeptides.