Crystallographic characterization of tryptophan-containing peptide 3(10)-helices.

Abstract

The molecular and crystal structures of four peptides containing one L-Trp guest residue in Aib (alpha-aminoisobutyric acid or C alpha-methyl alanine) host oligopeptide chains have been determined by X-ray diffraction. The peptides are Z-Aib-L-Trp-Aib-OMe, Z-(Aib)2-L-Trp-Aib-OMe, Z-(Aib)3-L-Trp-Aib-OtBu and Boc-(Aib)3-L-Trp-Aib-OMe. Right-handed beta-turns and incipient and fully developed 3(10)-helices are formed in the crystal state by the tri-, tetra- and pentapeptides, respectively. The Trp residue is easily accommodated in these folded structures. The average geometry and preferred conformation for the Trp indolyl side chain are also discussed.