Abstract
Oligomers of β-substituted β-amino acids ('β3-peptides') are known to adopt a helical secondary structure defined by 14-membered ring hydrogen bonds ('14-helix'). Here, we describe a deca-β3-peptide, 1, that does not adopt the 14-helical conformation and that may prefer an alternative secondary structure, β3-Peptide 1 is composed exclusively of residues with side chains that are not branched adjacent to the β-C-atom β3-hLeu, β3-hLys, and β3-hTyr). In contrast, an analogous β3-peptide, 2, containing β3-hVal residues in place of the β3-hLeu residues of 1, adopts a 14-helical conformation in MeOH, according to CD data. These results illustrate the importance of side-chain branching in determining the conformational preferences of β3-peptides.
Original language | English (US) |
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Pages (from-to) | 4154-4164 |
Number of pages | 11 |
Journal | Helvetica Chimica Acta |
Volume | 85 |
Issue number | 12 |
DOIs | |
State | Published - 2002 |
Externally published | Yes |
ASJC Scopus subject areas
- Catalysis
- Biochemistry
- Drug Discovery
- Physical and Theoretical Chemistry
- Organic Chemistry
- Inorganic Chemistry