Peptides of aminoxy acids as foldamers.
This Feature Article summarizes our efforts in developing a new family of foldamers from alpha-, beta- and gamma-aminoxy acids. From a series of conformational studies, we demonstrate that peptides consisting of aminoxy acids adopt several well-defined secondary structures, such as alpha N-O turns (which feature an eight-membered-ring hydrogen bond), beta N-O turns (a nine-membered-ring hydrogen bond), gamma N-O turns (a ten-membered-ring hydrogen bond), 1.8(8) helices (consecutive homochiral alpha N-O turns), 7/8 helices (alternating alpha N-O turns and gamma-turns), 1.7(9) helices (consecutive beta N-O turns), reverse turns (consecutive heterochiral alpha N-O turns) and sheet-like structures.
Li
Xiang
X
Department of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, China.
Yang
Dan
D
D000596:Amino Acids / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D008958:Models, Molecular; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary
D000596:Amino Acids; D010455:Peptides