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Updated: Mar 13, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Linker dependent chirality of solvent induced self-assembled structures of porphyrin-α-helical peptide conjugates
Francesca Biscaglia1, Elisa Frezza1, Enrico Zurlo1
1Department of Chemical Sciences, University of Padova, I-35131 Padova, Italy. marina.gobbo@unipd.it.
Abstract:
The solvent-promoted aggregation of porphyrins covalently linked to medium length peptides occurs with the formation of chiral supramolecular structures if the peptide chain can adopt an α-helical secondary structure. The circular dichroism spectra of different porphyrin-peptide conjugates show that the chiral arrangement of the porphyrins in the aggregates does not depend on the screw-sense of the peptide helix. Experimental evidence and molecular dynamic simulations suggest that the linker between the porphyrin and the peptide helix is responsible for the overall chirality of supramolecular structures. In particular when the linker is a chiral α-amino acid it is possible to tune the morphology of the chiral aggregates by inverting the configuration of the chiral center.
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