Design and synthesis of glycosylated beta3-peptides capable of folding into the 3(14)-helical conformation in water.
Herein, we describe the synthesis of seven glycosylated beta(3)-peptides, 1-7, which were designed to adopt stable 3(14)-helical conformations in aqueous solution. Such molecules are representative for a novel class of functionalized foldamers in which a natural post-translational modification is attached to an unnatural peptidomimetic backbone. Conformational studies by CD spectroscopic measurements were performed in methanol and in water (pH 7). Additionally, the influence of temperature, pH, and concentration on the ability of glycosylated beta(3)-peptides to adopt stable helical conformations were investigated. The first NMR-derived solution state structure of a glycosylated beta(3)-peptide in water is also presented.
Norgren
Anna S
AS
Department of Biochemistry and Organic Chemistry, Uppsala University, Box 576, S-75123 Uppsala, Sweden.
Arvidsson
Per I
PI
D002942:Circular Dichroism; D006031:Glycosylation; D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D017510:Protein Folding; D014867:Water / Q000737:chemistry*
D010455:Peptides; D014867:Water