Open AccessPotential Foldamers Based on an ortho-Terphenyl Amino Acid
Author(s) -
Adam F. Kleman,
Deseree L. Dufek,
Theodore L. Fobe,
Darrell R. McCaslin,
Brian P. Cary,
Michael R. Shirts,
Samuel H. Gellman
Publication year - 2021
Publication title -
organic letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.94
H-Index - 239
eISSN - 1523-7060
pISSN - 1523-7052
DOI - 10.1021/acs.orglett.1c01592
Subject(s) - terphenyl , chemistry , hydrogen bond , residue (chemistry) , chloroform , circular dichroism , amino acid residue , stereochemistry , combinatorial chemistry , molecule , organic chemistry , peptide sequence , biochemistry , gene
We describe the synthesis and characterization of a new class of oligomers built from a terphenyl-based amino acid. These oligomeric amides are of interest because the adoption of specific conformations could potentially be driven by the coordinated formation of inter-residue hydrogen bonds and aromatic interactions. Although high-resolution structural data have proven inaccessible, circular dichroism and nuclear magnetic resonance studies suggest that the new oligomers fold concomitantly with discrete self-association in chloroform.