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1.
Spectrochim Acta A Mol Biomol Spectrosc ; 211: 132-140, 2019 Mar 15.
Artigo em Inglês | MEDLINE | ID: mdl-30530066

RESUMO

New hydrophilic fluorescent selective ion sensor based on phenazine and phthalazine moieties, 1,1'-(phenazine-2,3-diyl)-bis(3-(1,4-dihydroxyphthalazin-6-yl)urea) (1), has been designed, synthesized and characterized. Interestingly, sensor 1 exhibits prominent "turn-on" and "turn-off" fluorogenic signaling at 580 nm towards Fe2+ & AcO- and Sr2+ & Cu2+, respectively. The fluorescence titration experiments shed light on the nature of the interaction between 1 and guest molecules (Fe2+, Sr2+, Cu2+ and AcO-), which divulge that 1 is flexible enough to orient itself according to the size of the guest molecule. Water mediated excited-state intramolecular proton transfer (ESIPT) and photo-induced electron transfer (PET) mechanisms are responsible for the dual behavior of 1, which binds with guest molecules in 1:1 stoichiometry. Based on the significant duplex fluorescence response of 1, a molecular logic gate keypad lock with sixteen "on" passwords for a storage system has been developed.

2.
J Photochem Photobiol B ; 183: 374-384, 2018 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-29763760

RESUMO

Binding interaction of Bovine Serum Albumin (BSA) with newly prepared rhodamine 6G-capped gold nanoparticles (Rh6G-Au NPs) under physiological conditions (pH 7.2) was investigated by a wide range of photophysical techniques. Rh6G-Au NPs caused the static quenching of the intrinsic fluorescence of BSA that resulted from the formation of ground-state complex between BSA and Rh6G-Au NPs. The binding constant from fluorescence quenching method (Ka = 1.04 × 104 L mol-1; LoD = 14.0 µM) is in accordance with apparent association constant (Kapp = 1.14 × 101 M-1), which is obtained from absorption spectral studies. Förster resonance energy transfer (FRET) efficiency between the tryptophan (Trp) residue of BSA and fluorophore of Rh6G-Au NPs during the interaction was calculated to be 90%. The free energy change (ΔG = -23.07 kJ/mol) of BSA-Rh6G-Au NPs complex was calculated based on modified Stern-Volmer Plot. The time-resolved fluorescence analysis confirmed that quenching of BSA follows static mechanism through the formation of ground state complex. Furthermore, synchronous and three-dimensional fluorescence measurement, Raman spectral analysis and Circular Dichroism spectrum results corroborate the strong binding between Rh6G-Au NPs and BSA, which causes the conformational changes on BSA molecule. In addition, fluorescence imaging experiments of BSA in living human breast cancer (HeLa) cells was successfully demonstrated, which articulated the value of Rh6G-Au NPs practical applications in biological systems.


Assuntos
Ouro/química , Nanopartículas Metálicas/química , Rodaminas/química , Soroalbumina Bovina/química , Animais , Varredura Diferencial de Calorimetria , Bovinos , Dicroísmo Circular , Transferência Ressonante de Energia de Fluorescência , Células HeLa , Humanos , Imagem Óptica , Soroalbumina Bovina/metabolismo , Análise Espectral Raman , Termogravimetria , Triptofano/química
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