Rectification of excitation with bathochromic shift induced by intense absorption of organic ligands during emission measurement of Eu(III) complex

Zhao, Hui; Su, Wei; Luo, Yanhua; Ji, Yaohui; Li, Zengchang; Jiu, Hongfang; Liang, H.; Chen, Biao; Zhang, Qijin

doi:10.1016/j.saa.2006.01.018

Cited by 14 publications

(8 citation statements)

References 14 publications

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“…role played by b-diketonate molecules [18]. It can be seen that their maximal excitation wavelength are 410 and 413 nm for Eu(DBM) 3 with their maximal absorption spectra the excitation peaks red shift resulted from the structure of the instrument [19]. are somewhat similar to each other.…”

Section: Synthesis Of Eu 2 (Ddbm) 3 H 2 Omentioning

confidence: 74%

Judd–Ofelt treatment on luminescence of europium complexes with β-diketone and bis(β-diketone)

Luo

Chen

et al. 2009

Journal of Luminescence

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Section: Synthesis Of Eu 2 (Ddbm) 3 H 2 Omentioning

confidence: 74%

Judd–Ofelt treatment on luminescence of europium complexes with β-diketone and bis(β-diketone)

Luo

Chen

et al. 2009

Journal of Luminescence

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“…Among these, fluorescence technique is a well known practical method for studying protein interactions with various ligands [12–14] as it yields a vast amount of information on binding characteristics and the microenvironment surrounding the protein residues.…”

Section: Introductionmentioning

confidence: 99%

Interaction of Bioactive Coomassie Brilliant Blue G with Protein: Insights from Spectroscopic Methods

Katrahalli

Kalanur²,

Seetharamappa³

2010

Sci. Pharm.

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The binding of coomassie brilliant blue G (CBB) to bovine serum albumin (BSA) was investigated under simulative physiological conditions employing different optical spectroscopic techniques viz., fluorescence emission, UV–visible absorption and FTIR. Fluorescence quenching data obtained at different temperatures suggested the presence of dynamic type of quenching mechanism. The binding constant of CBB-BSA and the number of binding sites (n) for CBB in BSA were calculated and found to be 4.20 × 104 M−1 and 0.96 respectively, at 302 K. The value of n close to unity indicated that the protein has a single class of binding sites for CBB. The thermodynamic parameters revealed that the hydrophobic forces played a major role in the interaction of CBB to BSA. The distance between the CBB and protein was calculated using the theory of Föster’s Resonance Energy Transfer (FRET). The conformational change in the secondary structure of BSA upon interaction with dye was investigated by synchronous fluorescence and FTIR techniques. Competitive binding studies were also carried out to know the location of binding of CBB on BSA.

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“…In the present report we focus on a newly synthesized indanedione derivative, 2-(2-hydroxy-3-ethoxybenzylidene)-1,3-indanedione (HEBID), studying its interaction with human and bovine serum albumins (HSA and BSA) by means of fluorescence and circular dichroism spectroscopies. Fluorescence is a practical method for studying protein interactions with various ligands [ 18 , 19 , 20 , 21 , 22 , 23 , 24 ], as it yields a vast amount of information on the magnitude of binding and on the microenvironment surrounding the protein residues. In our work, we monitored the changes in the intrinsic fluorescence of the SAs upon binding to HEBID.…”

Section: Introductionmentioning

confidence: 99%

Spectroscopic Investigations of the Binding Interaction of a New Indanedione Derivative with Human and Bovine Serum Albumins

et al. 2009

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Binding of a newly synthesized indanedione derivative, 2-(2-hydroxy-3-ethoxybenzylidene)-1,3-indanedione (HEBID), to human and bovine serum albumins (HSA and BSA), under simulated physiological conditions was monitored by fluorescence spectroscopy. The binding parameters (binding constants and number of binding sites) and quenching constants were determined according to literature models. The quenching mechanism was assigned to a Förster non-radiative energy transfer due to the HEBID-SA complex formation. A slightly increased affinity of HEBID for HSA was found, while the number of binding sites is approximately one for both albumins. The molecular distance between donor (albumin) and acceptor (HEBID) and the energy transfer efficiency were estimated, in the view of Förster’s theory. The effect of HEBID on the protein conformation was investigated using circular dichroism and synchronous fluorescence spectroscopies. The results revealed partial unfolding in the albumins upon interaction, as well as changes in the local polarity around the tryptophan residues.

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Rectification of excitation with bathochromic shift induced by intense absorption of organic ligands during emission measurement of Eu(III) complex

Cited by 14 publications

References 14 publications

Judd–Ofelt treatment on luminescence of europium complexes with β-diketone and bis(β-diketone)

Judd–Ofelt treatment on luminescence of europium complexes with β-diketone and bis(β-diketone)

Interaction of Bioactive Coomassie Brilliant Blue G with Protein: Insights from Spectroscopic Methods

Spectroscopic Investigations of the Binding Interaction of a New Indanedione Derivative with Human and Bovine Serum Albumins

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