Subdiffraction localization of a nanostructured photosensitizer in bacterial cells
Authors: Delcanale P., Pennacchietti F., Maestrini G., Rodríguez-Amigo B., Bianchini P., Diaspro A., Iagatti A., Patrizi B., Foggi P., Agut M., Nonell S., Abbruzzetti S., Viappiani C.
Autors Affiliation: Dipartimento di Fisica e Scienze della Terra, Università di Parma, Viale delle Scienze 7A, 43124 Parma, Italy; Dipartimento di Bioscienze, Università di Parma, Viale delle Scienze 11A, 43124 Parma, Italy; NEST, Istituto Nanoscienze, Consiglio Nazionale delle Ricerche, Piazza San Silvestro 12, 56127 Pisa, Italy; Fondazione Istituto Italiano di Tecnologia, Via Morego, 30, 16163 Genova, Italy; LENS (European Laboratory for Nonlinear Spectroscopy) Via N. Carrara 1, Sesto Fiorentino, Florence 50019, Italy; INO (Istituto Nazionale di Ottica), Largo Fermi 6, Florence 50125, Italy; Dipartimento di Chimica, Università di Perugia, via Elce di Sotto 8, Perugia, 06123 Italy; Institut Quimic de Sarrià, Universitat Ramon Llull, Via Augusta 390, 08017 Barcelona, Spain
Abstract: Antibacterial treatments based on photosensitized production of reactive oxygen species is a promising approach to address local microbial infections. Given the small size of bacterial cells, identification of the sites of binding of the photosensitizing molecules is a difficult issue to address with conventional microscopy. We show that the excited state properties of the naturally occurring photosensitizer hypericin can be exploited to perform STED microscopy on bacteria incubated with the complex between hypericin and apomyoglobin, a self-assembled nanostructure that confers very good bioavailability to the photosensitizer. Hypericin fluorescence is mostly localized at the bacterial wall, and accumulates at the polar regions of the cell and at sites of cell wall growth. While these features are shared by Gram-negative and Gram-positive bacteria, only the latter are effectively photoinactivated by light exposure.
Journal/Review: SCIENTIFIC REPORTS
Volume: 5 Pages from: 15564 to: 15564
More Information: This work has been partially supported by MiUR Programmi di Ricerca di Rilevante Interesse Nazionale PRIN 2010JFYFY2-002.DOI: 10.1038/srep15564Citations: 21data from “WEB OF SCIENCE” (of Thomson Reuters) are update at: 2020-10-18References taken from IsiWeb of Knowledge: (subscribers only)Connecting to view paper tab on IsiWeb: Click hereConnecting to view citations from IsiWeb: Click here