|Title||Effects of the alternating backbone configuration on the secondary structure and self-assembly of beta-peptides: 2006, J AM CHEM SOC, V128, P1162, DOI 10.1021/ja0547228|
|Publication Type||Journal Article|
|Year of Publication||2006|
|Authors||Martinek, TA, Mándity, IM, Fulop, L, Toth, GK, Vass, E, Hollósi, M, Forro, E, Fülöp, F|
|Journal||Journal of the American Chemical Society|
Heterochiral homo-oligomers with alternating backbone configurations were constructed by using the different enantiomers of the cis- and trans-2-aminocyclopentanecarboxylic acid (ACPC) monomers. Molecular modeling and the spectroscopic techniques (NMR, ECD, and VCD) unequivocally proved that the alternating heterochiral cis-ACPC sequences form an H10/12 helix, where extra stabilization can be achieved via the cyclic side chains. The ECD and TEM measurements, together with molecular modeling, revealed that the alternating heterochiral trans-ACPC oligomers tend to attain a polar-strand secondary structure in solution, which can self-assemble into nanostructured fibrils. The observations indicate that coverage of all the possible secondary structures (various helix types and strand-mimicking conformations) can be attained with the help of cyclic beta-amino acid diastereomers. A relationship has been established between the backbone chirality pattern and the prevailing secondary structure, which underlines the role of stereochemical control in the beta-peptide secondary structure design and may contribute to future biological applications.