In this work, we examine the electronic and morphological consequences of constitutional isomerism in tri- and tetrablock biohybrid self-assembling molecules that display three regimes of "hydrophobic" composition. A solubilizing hydrophilic peptide head group is attached covalently to a pi-conjugated oligothiophene unit that undergoes pi-pi stacking interactions and introduces a unique quadrupolar character, a hydrophobic peptide segment that encourages hydrogen bonding, and in some cases, a terminal n-alkyl tail that further triggers hydrophobic collapse. We examine constitutional isomerism by swapping the presentation of these disparate hydrophobic blocks in these complex pi-conjugated peptides. We found that constitutional isomerism in molecules containing two peptide segments and the pi-conjugated oligomer greatly impacts solubility, nanostructure lateral bundling, and the mode of molecular packing that ultimately dictates electronic communication among the pi-conjugated units. Furthermore, we found that this effect is not diluted by the addition of an n-alkyl tail that also provides access to a range of nanoarchitectures from spheres to elongated micellar structures, rods, and ribbons.