ja0607133_si_001.pdf (3.94 MB)
Carbohydrate Amino Acids: The Intrinsic Conformational Preference for a β-Turn-Type Structure in a Carbopeptoid Building Block
journal contribution
posted on 2006-12-27, 00:00 authored by Rebecca A. Jockusch, Francis O. Talbot, Paul S. Rogers, Michela I. Simone, George W. J. Fleet, John P. SimonsInfrared ion-dip spectroscopy coupled with DFT and ab initio calculations are used to establish
the intrinsic conformational preference of the basic structural unit of a peptide mimic, a cis-tetrahydrofuran-based “carbopeptoid” (amide−sugar−amide), isolated at low temperature in the gas phase. The carbopeptoid
units form a β-turn-type structure, stabilized by an intramolecular NH → OC hydrogen bond across the
sugar ring, thus forming a 10-membered, C10 turn. Despite the clear preference for C10 β-turn structures in
the basic unit, however, the presence of multiple hydrogen-bond donating and accepting groups also
generates a rich conformational landscape, and alternative structures may be populated in related molecules.
Calculations on an extended, carbopeptoid dimer unit, which includes an alternating amide−sugar−amide−sugar−amide chain, identify conformers exhibiting alternative hydrogen-bonding arrangements that are
somewhat more stable than the lowest-energy double β-turn forming conformer.