Conformational Heterogeneity, Self-Assembly, and Gas Adsorption Studies of Isomeric Hybrid Peptides

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.