Abstract
The folding and self-assembly propensities of three synthetic isomeric aliphatic–aromatic backbone hybrid peptides are illustrated. Single crystal X-ray diffraction studies of three isomeric hybrid dipeptides Boc-Phe-x-aminobenzoic acid (x = o/m/p) reveal that the peptides adopt unconventional conformations which self-assemble to form diverse supramolecular architectures using hydrogen bonding interactions and other noncovalent interactions in the solid state. The N2 sorption propensities of the isomeric hybrid peptides in the solid state significantly vary with folding and self-assembly nature. The peptides 1 and 2 exhibit type-III N2 sorption isotherm, though peptide 1 adsorbs 2-fold higher N2 than does peptide 2.
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