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RESEARCH PRODUCT
Impact of the ΔPhe configuration on the Boc-Gly-ΔPhe-NHMe conformation: experiment and theory
Aneta BuczekDawid SiodłakMaciej BujakMałgorzata A. BrodaTeobald KupkaMaciej Makowskisubject
Diffractionβ-turn tendencyCrystal structure010402 general chemistry01 natural sciencesGas phaseX-ray crystal structure analysischemistry.chemical_compoundResidue (chemistry)Peptide conformational analysisZ isomer0103 physical sciencesPhysical and Theoretical Chemistry13C NMRChloroform010304 chemical physicsDehydrophenylalanineE isomer1H NMRCondensed Matter Physics0104 chemical sciencesSolventCrystallographychemistryIR spectroscopyDFT-GIAO calculationsSingle crystaldescription
Conformational propensities of N-t-butoxycarbonyl-glycine-(E/Z)-dehydrophenylalanine N′-methylamides (Boc-Gly-(E/Z)-ΔPhe-NHMe) in chloroform were investigated by NMR and IR techniques. The low-temperature crystal structure of the E isomer was determined by single crystal X-ray diffraction and the experimental data were elaborated by theoretical calculations using DFT (B3LYP, M06-2X) and MP2 approaches. The β-turn tendencies for both isomers were determined in the gas phase and in the presence of solvent. The obtained results reveal that the configuration of ΔPhe residue significantly affects the conformations of the studied dehydropeptides. The tendency to adopt β-turn conformations is significantly lower for the E isomer (Boc-Gly-(E)-ΔPhe-NHMe), both in gas phase and in chloroform solution.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2019-07-18 | Structural Chemistry |