Self-assembling of the porphyrin-linked acyclic penta- and heptapeptides in aqueous trifluoroethanol

The conjugates of porphyrin with links to the acyclic penta- and heptapeptides were synthesized to mimic natural multiple porphyrin systems. The linear penta- and heptapeptide with hydrophilic/ hydrophobic alternative sequences took a random structure in aqueous trifluoroethanol (TFE). However, these polypeptides took a beta-sheet structure in the same solvent when the N-terminal Cys linked to the porphyrin, suggesting that the conjugates self-assembled via the intermolecular hydrophobic interaction between the porphyrins. The circular dichroism (CD) spectra, UV/vis spectra, size exclusion chromatography (SEC), and H-1 NMR spectroscopy supported the self-assembling. In the self-assembled structure of the pentapeptide linking porphyrin at the p-phenyl position (9), the porphyrins were involved in two porphyrin-porphyrin interactions, i.e., the side-by-side interaction between the neighboring polypeptide chains and the face-to-face interaction between the first and the third peptide chains. The CD spectra of 9 showed two sets of Cotton effects probably arising from these two interactions. The UV/vis spectra also supported the above interpretation, showing multiple absorptions in the longwave and shortwave shifted regions. The SEC analyses showed the assembled structure of the conjugates. The H-1 NMR signals of the porphyrin rings of 9 were hardly observed in D2O-CD3OD because of the shortened spin-spin relaxation time T-2.