Structure and spectroscopy of E and Z isomers of Boc-Gly-Phe-NHMe | Abstract
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Structure and spectroscopy of E and Z isomers of Boc-Gly-Phe-NHMe

Author(s): Ma�?gorzata A Broda, Teobald Kupk and Aneta Buczek

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. Biological activity of numerous small size molecules is directly related to their conformational properties. It is possible to control pharmaco-kinetic properties of naturally occurring peptides by introduction of nonstandard amino acid residues into their backbone chain which could produce derivatives showing more desired pharmacological properties, for example, resistance to enzymatic degradation, receptor selectivity, enhanced potency, or bioavailability. For example, it is possible to introduce a dehydroamino acid residue and forcing a specific conformation of the chain fragment.