α,β-Dehydro-amino acid residues in the design of peptide structures. Molecular and crystal structures of two folded dehydro peptides
1992; Elsevier BV; Volume: 14; Issue: 1 Linguagem: Inglês
10.1016/s0141-8130(05)80015-7
ISSN1879-0003
AutoresV. Busetti, Marco Crisma, Claudio Toniolo, Severo Salvadori, Gianfranco Balboni,
Tópico(s)Protein Structure and Dynamics
ResumoThe molecular and crystal structures of two Nα-protected tripeptide amides, containing in the central position the α-β-dehydro-amino acid residue ΔPhe (Z-configurational isomer), were determined by X-ray diffraction. While Z-Gly-ΔPhez-l-Pro-NH2 is characterized in the crystal state by the presence of a type I β-bend conformation (at the ΔPhez-l-Pro sequence), Z-d-Ala-ΔPhez-Gly-NH2 is folded into two consecutive β-bends (type II′ followed by type I), at the d-Ala-ΔPhez and ΔPhez-Gly sequences, respectively. In both cases the achiral ΔPhez residue adopts a set of , ψ angles typical of the right-handed helical conformation. The ΔPhe residue may be exploited to design aromatic peptides with preferred secondary structures.
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