[Lysine residue as an amino acid substitute for conformational constraint of Xaa-Asp fragment of biologically active peptides using side chain lactamization].
The model cyclopeptide Ac-Lys-Asp-NHMe was used to test Lys as a possible substitute for Xaa in peptide fragment Xaa-Asp whose conformational mobility would be constrained by lactamization of the Lys and Asp side chains. By means of theoretical conformational analysis, such a lactam was shown to be capable of fixing several conformations of the peptide. Among them, 32 conformations corresponded to 8 low-energy regions of the linear peptide Ac-Ala-Asp-NHMe, which was chosen as a model for the peptide fragment Xaa-Asp. In this case, the conformational possibilities of the Xaa residue were constrained to two regions of the Phi, Psi-map, (A + G) and C according to Zimmermann-Sheraga notation.
Kostetskiĭ
P V
PV
Artem'ev
I V
IV
D001224:Aspartic Acid / Q000737:chemistry*; D008239:Lysine / Q000737:chemistry*; D010456:Peptides, Cyclic / Q000737:chemistry*; D011487:Protein Conformation
D010456:Peptides, Cyclic; D001224:Aspartic Acid; D008239:Lysine