The first x-ray diffraction structure analysis of a C-alpha-ethyl, C-alpha-benzylglycine [(alpha Et)Phe]-containing peptide, N-alpha-benzyl-oxycarbonyl-alpha-aminoisobutyryl-alpha-amino-isobutyryl-(S)-C-alpha-ethyl, C-alpha-benzylglycal-alpha-aminoisobutyric acid (methanol solvate), has been performed. In the crystal state the N-alpha-protected tetrapeptide is folded iii all incipient, left-handed 3(10)-helical structure. This finding confirms that the relationship between (alpha Et)Phe alpha-carbon chirality and screw sense of the helix that is formed is opposite to that exhibited by protein amino acids, including Phe.
(s)-c-alpha-ethyl, C-alpha-benzylglycine [(s)-(alpha-et)phe] Peptides Fold In Left-handed Helical Structures
FORMAGGIO, FERNANDO;TONIOLO, CLAUDIO;
1995
Abstract
The first x-ray diffraction structure analysis of a C-alpha-ethyl, C-alpha-benzylglycine [(alpha Et)Phe]-containing peptide, N-alpha-benzyl-oxycarbonyl-alpha-aminoisobutyryl-alpha-amino-isobutyryl-(S)-C-alpha-ethyl, C-alpha-benzylglycal-alpha-aminoisobutyric acid (methanol solvate), has been performed. In the crystal state the N-alpha-protected tetrapeptide is folded iii all incipient, left-handed 3(10)-helical structure. This finding confirms that the relationship between (alpha Et)Phe alpha-carbon chirality and screw sense of the helix that is formed is opposite to that exhibited by protein amino acids, including Phe.
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