Synthesis, spectroscopic, and photophysical characterization and photosensitizing activity toward prokaryotic and eukaryotic cells of porphyrin-magainin and -buforin conjugates

Ryan Dosselli, Rubén Ruiz-González, Francesca Moret, Valentina Agnolon, Chiara Compagnin, Maddalena Mognato, Valentina Sella, Montserrat Agut, Santi Nonell, Marina Gobbo, Elena Reddi

Producción científica: Artículo en revista indizadaArtículorevisión exhaustiva

46 Citas (Scopus)

Resumen

Cationic antimicrobial peptides (CAMPs) and photodynamic therapy (PDT) are attractive tools to combat infectious diseases and to stem further development of antibiotic resistance. In an attempt to increase the efficiency of bacteria inactivation, we conjugated a PDT photosensitizer, cationic or neutral porphyrin, to a CAMP, buforin or magainin. The neutral and hydrophobic porphyrin, which is not photoactive per se against Gram-negative bacteria, efficiently photoinactivated Escherichia coli after conjugation to either buforin or magainin. Conjugation to magainin resulted in the considerable strengthening of the cationic and hydrophilic porphyrin's interaction with the bacterial cells, as shown by the higher bacteria photoinactivation activity retained after washing the bacterial suspension. The porphyrin-peptide conjugates also exhibited strong interaction capability as well as photoactivity toward eukaryotic cells, namely, human fibroblasts. These findings suggest that these CAMPs have the potential to carry drugs and other types of cargo inside mammalian cells similar to cell-penetrating peptides.

Idioma originalInglés
Páginas (desde-hasta)1403-1415
Número de páginas13
PublicaciónJournal of Medicinal Chemistry
Volumen57
N.º4
DOI
EstadoPublicada - 27 feb 2014

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