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Regularly alternating L , D ‐peptides. III. Hexacyclic peptides from valine or phenylalanine
Author(s) -
Pavone Vincenzo,
Benedetti Ettore,
Di Blasio Benedetto,
Lombardi Angela,
Pedone Carlo,
Tomasich Lera,
Lorenzi Gian Paolo
Publication year - 1989
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360280123
Subject(s) - chemistry , molecule , trifluoroacetic acid , stereochemistry , peptide , hydrogen bond , cyclic peptide , metal , amino acid , valine , phenylalanine , crystallography , organic chemistry , biochemistry
In the present paper we describe the single‐crystal x‐ray analyses of two cyclic hexapeptides containing an equal number of alternating L,D‐residues as putative analogues of the metal binding compounds, enniatin and beauvericine. Both the molecules of c( L ‐Val‐ D ‐Val) 3 and c( L ‐Phe‐ D ‐Phe) 3 retain in the solid state the center of symmetry and crystallize with six and eight trifluoroacetic acid molecules, respectively. The peptides are strongly hydrogen bonded to the solvent molecules. We estimate, on the basis of the molecular geometry and spatial arrangement of the peptide carbonyl groups and in comparison with other metal binding cyclic peptides, the ability of these molecules to interact with metal ions as 1:1 complexes.