We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
β-Strand Mimetic Foldamers Rigidified through Dipolar Repulsion.
- Authors
German, Elizabeth A.; Ross, Jonathan E.; Knipe, Peter C.; Don, Michaela F.; Thompson, Sam; Hamilton, Andrew D.
- Abstract
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.
- Subjects
COORDINATE covalent bond; PROTEIN-protein interactions; ENTHALPY; COVALENT bonds; CHEMICAL research
- Publication
Angewandte Chemie, 2015, Vol 127, Issue 9, p2687
- ISSN
0044-8249
- Publication type
Article
- DOI
10.1002/ange.201410290