Tuning the morphology of mesoscopic structures of porphyrin macrocycles functionalized by an antimicrobial peptide
The aggregation properties of two peptide-porphyrin conjugates were investigated by optical spectroscopy and microscopy imaging with nanometer resolution. Specifically, a tetraphenylporphyrin platform was functionalized by (L)-magainin, a 23-residue long antimicrobial peptide, and by a (L)-magainin analogue differing from the parent peptide by a single residue substitution, i.e. an Ala vs. Phe replacement in the position 5 of the peptide chain.