The crystal structure of Afc-containing peptide(936 views) Lombardi A, De Simone G, Galdiero S, Nastri F, Di Costanzo L, Makihiara K, Yamada T, Pavone V
Keywords: C(α, α)-Disubstituted Amino Acids, Conformation, Crystal Structure, Peptide, Amino Acid Sequence, Article, Protein Conformation, Protein Folding, Structure Activity Relation, X Ray Crystallography, X-Ray, Fluorenes, Glycine, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Oligopeptides, Protein Structure, Synthesis, Dipeptides,
Affiliations: Ctro. Interuniversitario di Ric., Ctro. di Stud. di B., University of Napoli Federico II, via Mezzocannone 4, I-80134 Napoli, Italy
Department of Chemistry, Faculty of Science, Konan University, 658 Kobe, Japan
References: Not available.
The crystal structure of Afc-containing peptide
A systematic structural analysis of Afc (9-amino-fluorene-9-carboxylic acid) containing peptides is here reported. The crystal structures of four fully protected tripeptides containing the Afc residue in position 2: Z-X1- Afc2-Y3-OMe (peptide a: X = Y = Gly; peptide b: X = Aib, C(α,α)- dimethylglycine, Y = Gly; peptide c: X = Gly, Y = Aib; peptide d: X = Y = Aib) have been solved by x-ray crystallography. All the results suggest that the Afc residue has a high propensity to assume an extended conformation. In fact, the Afc residue adopts an extended conformation in three peptides examined in this paper (peptides a-c). In contrast, Afc was found in a folded conformation, in the 310-helical region, only in the peptide d, in which it is both preceded and followed by the strong helix promoting Aib. (C) 2000 John Wiley and Sons, Inc.
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