Nonpeptidic foldamers from amino acids: synthesis and characterization of 1,3-substituted triazole oligomers.
Nonpeptidic foldamers capable of displaying protein-like functionality were prepared by swapping amide bonds with 1,2,3-triazole rings. The overall conformation of these triazole oligomers is largely dictated by dipole-dipole interactions between adjacent rings. Solution NMR studies suggest that a zigzag conformation, which closely mimics the beta-strand structure, predominates in two different tetramers.
Angelo
Nicholas G
NG
Department of Chemistry, New York University, New York, New York 10003, USA.
Arora
Paramjit S
PS
D000596:Amino Acids / Q000737:chemistry*; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry*; D011487:Protein Conformation; D014230:Triazoles / Q000138:chemical synthesis* / Q000737:chemistry
D000596:Amino Acids; D010455:Peptides; D014230:Triazoles