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1.
Phys Chem Chem Phys ; 16(13): 5933-6, 2014 Apr 07.
Artigo em Inglês | MEDLINE | ID: mdl-24549369

RESUMO

A unique pH-driven Förster resonance energy transfer (FRET) based biosensor emission by a pyrazoline-doxorubicin pair has been deciphered with a bioimaging application in a live HepG2 cell whereas conformational switching of both molecules at elevated pH reveals a fascinating twist (FRET-OFF) via strong fluorescent exciplex formation.


Assuntos
Técnicas Biossensoriais , Doxorrubicina/química , Pirazóis/química , Transferência Ressonante de Energia de Fluorescência , Células Hep G2 , Humanos , Concentração de Íons de Hidrogênio , Microscopia Confocal
2.
J Nanosci Nanotechnol ; 12(3): 2229-38, 2012 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-22755042

RESUMO

Polycrystalline lanthanum oxalate (LaOX) nanorods (NRs) were succesfully synthesized using reverse micellar (RM) method. The study espouses the versatility of the reverse micellar method forming monodisperse, stable nanorods at room temperature. The as-synthesized LaOX nanorods were characterised by different techniques. Result shows that the nanorods of LaOX with aspect ratio 10.2:1 have preferred growth direction of (020). The pure phase synthesis of the nanorods was confirmed from Fourier transformed infrared (FTIR) and X-ray diffraction (XRD) analysis. The thermo gravimetric analysis (TGA) and differential thermal analysis (DTA) of the as-synthesized nanorods were perfomed to observe their thermal degradation. Synthesized nanorods are fluorescent having emission maximum at 329 nm. Fluorescence resonance energy transfer (FRET) phenomenon has been observed between LaOX nanorods (energy donor) and naphthalimide (NAP) derivative (energy acceptor) and this mechanism can be helpful for sensing of NAP or NAP like molecules used as antioxidative in living systems.

3.
J Phys Chem A ; 115(33): 9169-79, 2011 Aug 25.
Artigo em Inglês | MEDLINE | ID: mdl-21766855

RESUMO

This paper investigates how solution conditions, especially solvent polarity and hydrogen bonding, influence the fluorescence of an anticancer drug, doxorubicin hydrochloride (DOX). When excited at 480 nm, this molecule shows single fluorescence. However, when excited at 346 nm, it shows dual fluorescence. The ground and excited state intramolecular double proton transfer in DOX has been observed and investigated to shed light on their corresponding spectroscopy and dynamics in different protic and aprotic solvents. An increase in pH results in enhancement of emission from the ionic conformer with parallel dwindling of emission of the neutral species. Based on the experimental and theoretical studies on DOX, a ground and excited state intramolecular double proton transfer mechanism is proposed to explain the unusual excitation-dependent dual fluorescence of DOX.


Assuntos
Antineoplásicos/química , Doxorrubicina/química , Fluorescência , Ligação de Hidrogênio , Concentração de Íons de Hidrogênio , Cinética , Luz , Modelos Moleculares , Processos Fotoquímicos/efeitos da radiação , Prótons , Soluções , Solventes/química , Espectrometria de Fluorescência , Termodinâmica
4.
J Phys Chem A ; 115(11): 2216-24, 2011 Mar 24.
Artigo em Inglês | MEDLINE | ID: mdl-21366260

RESUMO

The solvatochromic behavior of two newly synthesized naphthalimide derivatives (I and II) which have potential antioxidative activities in anticarcinogenic drug development treatment, has been monitored in protic and aprotic solvents of different polarity applying steady-state and time-resolved fluorescence techniques. The compounds exhibit unique photophysical response in different solvent environments. The spectral trends do not appear to originate only from changes in the solvent polarity but also indicate that hydrogen bonding interactions and intramolecular charge transfer (ICT) influence the energy of electronic excitation of the compounds. Incorporation of an amino group at C(4) position of the naphthalimide ring in II makes it behave differently from I in terms of spectral characterization and fluorescence efficacy of the systems. The nonradiative relaxation process of the compounds is governed by medium polarity. The ground state geometry, lowest energy transition, and the UV-vis absorption energy of the compounds were studied using density functional theory (DFT) and time-dependent density functional theory (TDDFT) at the B3LYP/6-31G* level, which showed that the calculated outcomes were in good agreement with experimental data.


Assuntos
Ligação de Hidrogênio , Naftalimidas/química , Solventes/química , Antineoplásicos , Antioxidantes/síntese química , Antioxidantes/química , Elétrons , Transferência de Energia , Modelos Moleculares , Naftalimidas/síntese química
5.
J Photochem Photobiol B ; 129: 69-77, 2013 Dec 05.
Artigo em Inglês | MEDLINE | ID: mdl-24177206

RESUMO

The principal intent of the present contribution is to decipher the binding domain and structural changes of trypsin (TPS), a proteolytic globular enzyme and two serum proteins, namely, bovine serum albumin (BSA), human serum albumin (HSA) association with a newly synthesized bioactive isoquinolindione derivative (ANAP) by employing steady state, time resolved fluorescence and circular dichroism (CD) techniques. Intramolecular charge transfer emission (ICT) of ANAP is found to be responsible for the commendable sensitivity of the probe as an extrinsic fluorescent marker to the protein environments. A sharp distinctive feature of determined micropolarities in proteinous media clearly demarcates the differential extent of hydrophobicity around the encapsulated ANAP. A proficient efficiency tunable fluorescence (Förster type) resonance energy transfer (FRET) from the excited tryptophan to ANAP reveals that ANAP binds in the close vicinity of the tryptophan residue in protein. Molecular modeling simulation has been exploited for evaluating the probable interaction site of ANAP in proteinous assembly which shows subdomain IIA are earmarked to possess affinity for ANAP in serum albumins whereas S1 binding pocket in TPS has been found potential binding region for ANAP.


Assuntos
Antioxidantes/metabolismo , Isoquinolinas/química , Substâncias Macromoleculares/química , Serina Proteases/metabolismo , Soroalbumina Bovina/metabolismo , Albumina Sérica/metabolismo , Animais , Antioxidantes/química , Sítios de Ligação , Bovinos , Dicroísmo Circular , Transferência Ressonante de Energia de Fluorescência , Humanos , Isoquinolinas/metabolismo , Lasers , Substâncias Macromoleculares/metabolismo , Simulação de Acoplamento Molecular , Ligação Proteica , Estrutura Terciária de Proteína , Serina Proteases/química , Albumina Sérica/química , Soroalbumina Bovina/química
6.
Artigo em Inglês | MEDLINE | ID: mdl-22446758

RESUMO

Spectroscopic studies of Naproxen (NP), a nonsteroidal drug have been carried out in well characterized, micellar media of cationic surfactants of a homologous series having general formula C(n)TAB (alkyl trimethyl ammonium bromide) and of nonionic surfactants of Igepal (Ig) series (poly(oxyethylene) nonyl phenol). The fluorescence behavior of the drug molecule in C(n)TAB micelles has been found to be opposite to that in Igepal micelles. The binding constants during probe micelle binding have been evaluated from relevant fluorescence data. Location and nature of the surrounding medium of the probe in micellar media have been ascertained from fluorescence quenching study. Fluorescence anisotropy parameter has been monitored for exploring the imposed motional restriction of the microenvironment around the probe. Contrasting behavior of the drug molecule has been observed in two different types of micelles. Based on the experimental and theoretical studies, an attempt has been made to explain the different behavior of the probe in different media.


Assuntos
Anti-Inflamatórios não Esteroides/química , Micelas , Naproxeno/química , Fenóis/química , Polietilenoglicóis/química , Polarização de Fluorescência , Tensoativos/química
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