Study on the interaction of La3+ with bovine serum albumin at molecular level

Yuan, Dong; Shen, Zhong-Lan; Liu, Rutao; Gao, Canzhu

doi:10.1016/j.jlumin.2011.06.036

Cited by 10 publications

(4 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…By the home-made FI-CL model [46], the binding constants K D and the number of binding sites n of BSA with La III , Eu III , Gd III , Tb III and Lu III are listed in Table 6. It could be seen K D were at 10 4 -10 5 level, suggesting that there existed a high binding affinity of Ln III to BSA, which agreed well with the results obtained by fluorescence quenching method [47][48][49]. The binding ability of Ln III increased in the sequence: La III oEu III oGd III o Tb III oLu III , which was highly related to Ln III expansion-inducing ability increased and steric effect decreased caused by lanthanide contraction [50].…”

Section: Determination Of Binding Parameters Of Bsa With Ln IIIsupporting

confidence: 79%

Study on the luminescence behavior of lanthanide ions with luminol by flow injection chemiluminescence analysis

Liu

Wang

et al. 2015

Journal of Luminescence

View full text Add to dashboard Cite

Section: Determination Of Binding Parameters Of Bsa With Ln IIIsupporting

confidence: 79%

Study on the luminescence behavior of lanthanide ions with luminol by flow injection chemiluminescence analysis

Liu

Wang

et al. 2015

Journal of Luminescence

View full text Add to dashboard Cite

“…In spite of this, more than 115 works has been published in recent years employing BSA as protein where the slope is equated to the number of sites. These works comprise from ions to surfactants and metal complexes .…”

Section: Resultsmentioning

confidence: 99%

Evaluation of the Number of Binding Sites in Proteins from their Intrinsic Fluorescence: Limitations and Pitfalls

Lissi

Calderón

Campos

2013

Photochem & Photobiology

View full text Add to dashboard Cite

Changes in the intrinsic protein fluorescence with the additive concentration provide one of the most employed methodologies for the evaluation of the binding constant and the number of binding sites. In the last years, more than 175 studies have been published where the double logarithmic plot shown below is used toward determining the number of equivalent binding sites (n). Log [(F° - F)/F] = log K + n log [Q0 ]. However, the value of n evaluated by this procedure is unrelated to the number of equivalent binding sites; rather it represents the stoichiometry of the binding step. The confusion on the meaning of n arises upon assuming that the binding process is represented by the forward and backward elementary steps shown below, implying that binding of the n solutes takes place simultaneously, i.e. there are no intermediate species. nQ + P ⇆ Qn P. The conclusion that n is unrelated to the number of equivalent binding sites is supported by the fact that in all the systems considered (99% of them) n values are close to one and much smaller than those obtained by ultrafiltration. It is then remarkable, the profusion of publications in peer-reviewed, specialized journals including a conceptual error that confuses Hill's coefficient and/or the stoichiometry of the binding step with the number of independent binding sites. Here, we discuss the origin of this common misconception and provide alternative methods to determine the number of binding sites.

show abstract

“…Fluorescence quenching can proceed by different mechanisms, which are usually classified as either dynamic quenching or static quenching. For the dynamic quenching, as the temperature of the system rises, the effective collision time between molecules, the energy transfer efficiency and the fluorescence quenching constants of substances will all increase [16] . Whereas, for the static quenching, increasing temperature reduces the stability of complexes formed, resulting in the quenching constants decrease.…”

Section: Resultsmentioning

confidence: 99%

“…Taking the fluorescence lifetime of the biopolymer ( τ 0 ) as around 10 −8 s [16] , the values of K q could be obtained according to Eq. (2) .…”

Section: Resultsmentioning

confidence: 99%

Investigation of the interaction between indigotin and two serum albumins by spectroscopic approaches

Cheng

Zhao

et al. 2013

Journal of Pharmaceutical Analysis

View full text Add to dashboard Cite

The binding characteristics of indigotin with human serum albumin (HSA) and bovine serum albumin (BSA) have been investigated by various spectroscopic techniques. Spectroscopic analysis revealed that the quenching mechanism between indigotin and HSA/BSA belonged to the static quenching. The displacement experiments suggested that indigotin primarily bound to tryptophan residues on proteins within site I. The thermodynamic parameters indicated that the binding of indigotin–HSA/BSA mainly depended on the hydrophobic interaction. The binding distance of indigotin to HSA/BSA was evaluated. The results by synchronous fluorescence, three-dimensional fluorescence, Fourier Transform Infrared spectroscopy (FT-IR) and circular dichroism (CD) spectra showed that the conformation of proteins altered in the presence of indigotin.

show abstract

Study on the interaction of La3+ with bovine serum albumin at molecular level

Cited by 10 publications

References 29 publications

Study on the luminescence behavior of lanthanide ions with luminol by flow injection chemiluminescence analysis

Study on the luminescence behavior of lanthanide ions with luminol by flow injection chemiluminescence analysis

Evaluation of the Number of Binding Sites in Proteins from their Intrinsic Fluorescence: Limitations and Pitfalls

Investigation of the interaction between indigotin and two serum albumins by spectroscopic approaches

Contact Info

Product

Resources

About