Toward β-Peptide Tertiary Structure: Self-Association of an Amphiphilic 14-Helix in Aqueous Solution
- 1 November 2001
- journal article
- letter
- Published by American Chemical Society (ACS) in Organic Letters
- Vol. 3 (24) , 3963-3966
- https://doi.org/10.1021/ol016868r
Abstract
A major frontier in foldamer research is creation of unnatural oligomers that adopt discrete tertiary structures; at present, only biopolymers are known to fold into such compact conformations. We report an initial step toward helix-bundle tertiary structure in the β-peptide realm by showing that a 10-residue β-peptide designed to adopt an amphiphilic helical conformation forms small soluble aggregates in water. Sedimentation equilibrium data indicate that the aggregated state falls in the tetramer-hexamer size range.Keywords
This publication has 32 references indexed in Scilit:
- Protein design and folding: template trapping of self-assembled helical bundlesJournal of Peptide Science, 2001
- Solution Conformations of Helix-Forming β-Amino Acid HomooligomersJournal of the American Chemical Society, 2000
- The twists and turns of β‐peptidesChemical Biology & Drug Design, 1999
- Designing polymers that mimic biomoleculesCurrent Opinion in Structural Biology, 1999
- Synthesis and Characterization of trans-2-Aminocyclohexanecarboxylic Acid Oligomers: An Unnatural Helical Secondary Structure and Implications for β-Peptide Tertiary StructureJournal of the American Chemical Society, 1999
- De Novo Design and Structural Characterization of Proteins and MetalloproteinsAnnual Review of Biochemistry, 1999
- Formation of Short, Stable Helices in Aqueous Solution by β-Amino Acid HexamersJournal of the American Chemical Society, 1999
- (S)-β3-Homolysine- and (S)-β3-Homoserine-Containingβ-Peptides: CD Spectra in Aqueous SolutionHelvetica Chimica Acta, 1998
- Foldamers: A ManifestoAccounts of Chemical Research, 1998
- A self-replicating peptideNature, 1996