The self-association behavior of a newly characterized beta-strand-mimic, presented by an achiral nonproteinogenic model system Boc-gamma-Abz-NHMe (1: Boc = tert-butyloxycarbonyl; gamma-Abz = gamma-aminobenzoic acid; NHMe = N-methylamide), have been investigated using H-1 NMR and FT-IR absorption spectroscopy, in combination with computational ab initio calculations. The concentration dependence of H-1 NMR chemical shifts of the amide-NHs in CDCl3 exhibited noncooperative behavior of self-association, whereas the variable temperature 1H NMR chemical shifts data of the amide-NHs, i.e., temperature-coefficient (Delta delta/Delta T) values, could be accounted for by significant enhancement of self-association, i.e., aggregates higher than dimers. In the absence of N-H center dot center dot center dot O intramolecular H-bond in 1, the intense FT-IR absorption bands in informative amide-A region, i.e., N-H stretches at similar to 3465 and 3438 cm(-1) in chloroform solution, could be interpreted in terms of intermolecular H-bonding. The ab initio quantum mechanical calculations performed on two discrete isolated antiparallel H-bonded duplexes with a face-to-face and an edge-to-edge aromatic aromatic interaction provided strong support for their relative importance to stabilize favorable dimeric structures. The thermodynamic parameters deduced from van't Hoff plots, constructed from variable temperature H-1 NMR data of the amide-NHs in CDCl3, also substantiated the effectiveness of aromatic aromatic interactions for dimer formation and higher-order self-association. In view of the enormous structural importance of beta-strand-like building blocks in peptide design, we highlight intrinsic self-associating potentials of the readily available gamma-Abz moiety, besides the fact that such planar secondary structural mimics are presumed to offer greater prospective for constructing peptidomimetics and therapeutically relevant small molecules.