1229034-85-8Relevant academic research and scientific papers
Helix formation in preorganized β/γ-peptide foldamers: Hydrogen-bond analogy to the α-helix without α-amino acid residues
Guo, Li,Almeida, Aaron M.,Zhang, Weicheng,Reidenbach, Andrew G.,Choi, Soo Hyuk,Guzei, Ilia A.,Gellman, Samuel H.
supporting information; experimental part, p. 7868 - 7869 (2010/08/04)
We report the first high-resolution structural data for the β/γ-peptide 13-helix (i,i+3 CO...HN H-bonds), a secondary structure that is formed by oligomers with a 1:1 alternation of β- and γ-amino acid residues. Our characterization includes both crystallophaphic and 2D NMR data. Previous studies suggested that β/γ-peptides constructed from conformationally flexible residues adopt a different helical secondary structure in solution. Our design features preorganized β- and γ-residues, which strongly promote 13-helical folding by the 1:1 β/γ backbone.
