Preparation and conformational analysis of C-glycosyl beta(2)- and beta/beta(2)-peptides.
Ten C-glycosyl beta(2)- and beta/beta(2)-peptides with three to eight amino acid residues have been prepared. Solution and solid-phase peptide syntheses were employed to assemble beta(2)-amino acids in which C-glycosylic substituents are attached to the C-2 position of beta-amino acids. Conformational analysis of the C-glycosyl beta(2)-peptides using NMR and CD spectra indicates that the tripeptide can form a helical secondary structure. Besides, helix directions of the C-glycosyl beta/beta(2)-peptides are governed by the configuration at the alpha-carbon of the peptide backbone that originates from the stereocenter of the C-glycosyl beta(2)-amino acids.
Inaba
Yoko
Y
Department of Interdisciplinary Materials Science, Nara Women's University, Nara 630-8506, Japan.
Kawakami
Toru
T
Aimoto
Saburo
S
Ikegami
Takahisa
T
Takeuchi
Takae
T
Nakazawa
Takashi
T
Yano
Shigenobu
S
Mikata
Yuji
Y
D000596:Amino Acids / Q000737:chemistry*; D006020:Glycopeptides / Q000138:chemical synthesis* / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008956:Models, Chemical; D008968:Molecular Conformation; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*; D013237:Stereoisomerism
D000596:Amino Acids; D006020:Glycopeptides; D010455:Peptides