The present study reports the optical and photophysical properties of trans-A2B-corrole possessing pyrenyl unit attached at the meso-10-position and compares it with model trans-A2B-corrole having phenyl substituent at that position....

Novel 2-aryl(heteroaryl)-6-amino-4-(trifluoromethyl)quinoline scaffolds with promising photophysical, thermal and antimycobacterial properties are reported.

Two fluorinated meso-C6F5-corroles (5,15-bis(pentafluorophenyl)-10-(phenyl)corrole and 5,15-bis(pentafluorophenyl)-10-(1-pyrenyl)corrole) were biologically evaluated in terms of binding affinity to human serum albumin (HSA) and calf-thymus DNA (CT-DNA) via multiple spectroscopic techniques under physiological conditions combined with molecular docking calculations. The HSA:corrole interaction is spontaneous and moderate via static binding, disturbing both secondary and tertiary albumin structures at high fluorinated corrole concentrations. The competitive binding studies indicated positive cooperativity or allosteric activation, while molecular docking calculations suggested that both fluorinated corroles bind preferentially inside subdomains IIA and IB (sites I and III, respectively). The experimental CT-DNA binding assays indicated that fluorinated corroles interact spontaneously by non-classical modes in the minor groove of the CT-DNA strands via static fluorescence quenching mechanism. Molecular docking results also showed the minor groove as the main binding site for CT-DNA. Overall, the pyrene moiety increased the interaction with HSA and CT-DNA, which is probably due to the planarity and volume that favors the pyrene unit to be buried inside the biomacromolecule pockets.

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The design of new photosensitizers (PS) with improved properties is essential for the development of photodynamic therapy as an alternative therapeutic method.

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