β-Strand mimetic foldamers rigidified through dipolar repulsion.
Many therapeutically relevant protein-protein interactions contain hot-spot regions on secondary structural elements, which contribute disproportionately to binding enthalpy. Mimicry of such α-helical regions has met with considerable success, however the analogous approach for the β-strand has received less attention. Presented herein is a foldamer for strand mimicry in which dipolar repulsion is a central determinant of conformation. Computation as well as solution- and solid-phase data are consistent with an ensemble weighted almost exclusively in favor of the desired conformation.
['German|Elizabeth A|EA|', 'Ross|Jonathan E|JE|', 'Knipe|Peter C|PC|', 'Don|Michaela F|MF|', 'Thompson|Sam|S|', 'Hamilton|Andrew D|AD|']
D018360:Crystallography, X-Ray D008958:Models, Molecular D015394:Molecular Structure D010455:Peptides D017433:Protein Structure, Secondary D013816:Thermodynamics
protein-protein interactions peptidomimetics protein structures solid-state structures synthetic methods