New charge-bearing amino acid residues that promote β-sheet secondary structure.
Proteinogenic amino acid residues that promote β-sheet secondary structure are hydrophobic (e.g., Ile or Val) or only moderately polar (e.g., Thr). The design of peptides intended to display β-sheet secondary structure in water typically requires one set of residues to ensure conformational stability and an orthogonal set, with charged side chains, to ensure aqueous solubility and discourage self-association. Here we describe new amino acids that manifest substantial β-sheet propensity, by virtue of β-branching, and also bear an ionizable group in the side chain.
Department of Chemistry, University of Wisconsin , Madison, Wisconsin 53706, United States.
Stacy J
SJ
Maynard
Aaron M
AM
Almeida
Yasuharu
Y
Yoshimi
Samuel H
SH
Gellman
D000596:Amino Acids / Q000737:chemistry*; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D008968:Molecular Conformation; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012995:Solubility
D000596:Amino Acids; D010455:Peptides