1383809-50-4Relevant academic research and scientific papers
β-turn analogues in model αβ-hybrid peptides: Structural characterization of peptides containing β2,2Ac6c and β3,3Ac6c residues
Basuroy, Krishnayan,Rajagopal, Appavu,Raghothama, Srinivasarao,Shamala, Narayanaswamy,Balaram, Padmanabhan
, p. 1671 - 1678 (2012/10/07)
The effect of gem-dialkyl substituents on the backbone conformations of β-amino acid residues in peptides has been investigated by using four model peptides: Boc-Xxx-β2,2Ac6c(1- aminomethylcyclohexanecarboxylic acid)-NHMe (Xxx=Leu (1), Phe (2); Boc=tert-butyloxycarbonyl) and Boc-Xxx-β3,3Ac 6c(1-aminocyclohexaneacetic acid)-NHMe (Xxx=Leu (3), Phe (4)). Tetrasubstituted carbon atoms restrict the ranges of stereochemically allowed conformations about flanking single bonds. The crystal structure of Boc-Leu-β2,2Ac6c-NHMe (1) established a C 11 hydrogen-bonded turn in the αβ-hybrid sequence. The observed torsion angles (α(φ≈-60°, ψ≈-30°), β(φ≈-90°, θ≈60°, ψ≈-90°)) corresponded to a C11 helical turn, which was a backbone-expanded analogue of the type III β turn in αα sequences. The crystal structure of the peptide Boc-Phe-β3,3Ac6c-NHMe (4) established a C11 hydrogen-bonded turn with distinctly different backbone torsion angles (α(φ≈-60°, ψ≈120°), β(φ≈60°, θ≈60°, ψ≈-60°)), which corresponded to a backbone-expanded analogue of the type II β turn observed in αα sequences. In peptide 4, the two molecules in the asymmetric unit adopted backbone torsion angles of opposite signs. In one of the molecules, the Phe residue adopted an unfavorable backbone conformation, with the energetic penalty being offset by a favorable aromatic interaction between proximal molecules in the crystal. NMR spectroscopy studies provided evidence for the maintenance of folded structures in solution in these αβ-hybrid sequences. Copyright
