Folded polymers in Nature are made from relatively simple monomers, but they adopt complex folded structures through networks of non-covalent interactions. Nonnatural folded polymers, or foldamers, have the potential for similar versatility. Control of foldamer structure is crucial if these molecules are to realize their full potential as tools in biology and medicine. beta-3-Peptides have been shown to form stable helices, even without cyclic constraints. The logical next step in the study of such foldamer structures is to search for beta-3-peptides that can adopt well defined tertiary structures, such as helical bundles and coiled coils. We hope to use screening methods to identify peptides that can form parallel or antiparallel helical dimers from a library of beta-3-peptides. These experiments will begin to establish the rules of higher order structure formation of beta-3-peptide foldamers and open the door to designing more complex structures. ? ?
| Goodman, Jessica L; Petersson, E James; Daniels, Douglas S et al. (2007) Biophysical and structural characterization of a robust octameric beta-peptide bundle. J Am Chem Soc 129:14746-51 |
| Qiu, Jade X; Petersson, E James; Matthews, Erin E et al. (2006) Toward beta-amino acid proteins: a cooperatively folded beta-peptide quaternary structure. J Am Chem Soc 128:11338-9 |
