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β‐Strand Mimetic Foldamers Rigidified through Dipolar Repulsion
Author(s) -
German Elizabeth A.,
Ross Jonathan E.,
Knipe Peter C.,
Don Michaela F.,
Thompson Sam,
Hamilton Andrew D.
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201410290
Subject(s) - mimicry , foldamer , dipole , chemistry , crystallography , computational chemistry , physics , chemical physics , biophysics , biology , organic chemistry , ecology
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.