Folded polymers in Nature are made from relatively simple monomers, but they adopt complex foldedstructures through networks of non-covalent interactions. Nonnatural folded polymers, or foldamers, havethe potential for similar versatility. Control of foldamer structure is crucial if these molecules are to realizetheir 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 forbeta-3-peptides that can adopt well defined tertiary structures, such as helical bundles and coiled coils. Wehope to use screening methods to identify peptides that can form parallel or antiparallel helical dimers from alibrary of beta-3-peptides. These experiments will begin to establish the rules of higher order structureformation 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 |
