Diacid linkers that promote parallel beta-sheet secondary structure in water.
We report the development of diacid units that promote formation of a two-stranded parallel beta-sheet secondary structure between peptide segments attached via their N-termini. These linker units are formed by attaching glycine to one carboxyl group of cis-1,2-cyclohexanedicarboxylic acid (CHDA). Parallel sheet formation in water is observed when l-residue strands are attached to the CHDA-Gly unit with either of the two absolute configurations.
Department of Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.
Felix
F
Freire
John D
JD
Fisk
Aaron J
AJ
Peoples
Monika
M
Ivancic
Ilia A
IA
Guzei
Samuel H
SH
Gellman
D000143:Acids / Q000737:chemistry; D006860:Hydrogen Bonding; D015394:Molecular Structure; D017433:Protein Structure, Secondary; D012996:Solutions / Q000737:chemistry; D014867:Water / Q000737:chemistry*
D000143:Acids; D012996:Solutions; D014867:Water