6533b820fe1ef96bd127a405
RESEARCH PRODUCT
Two pentadehydropeptides with different configurations of the ΔPhe residues
Maciej MakowskiMarek LisowskiTadeusz LisAnna MaciągMaciej WiktorAnna Szlachcicsubject
chemistry.chemical_classificationMolecular StructureProtein ConformationOrganic CompoundsStereochemistryHydrogen bondPhenylalanineMolecular Sequence DataHydrogen BondingPhenylalanineGeneral MedicineCrystal structureCrystallography X-RayGeneral Biochemistry Genetics and Molecular BiologyAmino acidCrystallographyResidue (chemistry)Protein structurechemistryIntramolecular forceMoleculeAmino Acid SequenceOligopeptidesProtein Bindingdescription
Comparison of the crystal structures of two pentadehydropeptides containing DeltaPhe residues, namely (Z,Z)-N-(tert-butoxycarbonyl)glycyl-alpha,beta-phenylalanylglycyl-alpha,beta-phenylalanylglycine (or Boc(0)-Gly(1)-Delta(Z)Phe(2)-Gly(3)-Delta(Z)Phe(4)-Gly(5)-OH) methanol solvate, C(29)H(33)N(5)O(8) x CH(4)O, (I), and (E,E)-N-(tert-butoxycarbonyl)glycyl-alpha,beta-phenylalanylglycyl-alpha,beta-phenylalanylglycine (or Boc(0)-Gly(1)-Delta(E)Phe(2)-Gly(3)-Delta(E)Phe(4)-Gly(5)-OH), C(29)H(33)N(5)O(8), (II), indicates that the Delta(Z)Phe residue is a more effective inducer of folded structures than the Delta(E)Phe residue. The values of the torsion angles phi and psi show the presence of two type-III' beta-turns at the Delta(Z)Phe residues and one type-II beta-turn at the Delta(E)Phe residue. All amino acids are linked trans to each other in both peptides. Beta-turns present in the peptides are stabilized by intramolecular 4-->1 hydrogen bonds. Molecules in both structures form two-dimensional hydrogen-bond networks parallel to the (100) plane.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2009-12-16 | Acta Crystallographica Section C-Crystal Structure Communications |