Binding of several benzodiazepines to bovine serum albumin: Fluorescence study

Machicote, Roberta Grisel; Pacheco, María Emilia; Bruzzone, Liliana

doi:10.1016/j.saa.2010.06.020

Cited by 49 publications

(23 citation statements)

References 20 publications

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“…To shed light on the fluorescence quenching mechanism, fluorescence quenching data are analyzed by the Stern–Volmer equation, and quenching rate constants ( Kq ) for GSA and RbSA were listed in Table S1 (Supporting Information). All the Kq data were larger than the maximum value of collision quenching constant (2.0 × 10 10 l mol −1 s −1 ), which confirmed that the SA quenching processes were caused by static quenching mechanisms . Thus, association constant ( K a ) and the number of binding sites ( n ) can be obtained from the double‐logarithm curve on the basis of the static quenching Equation ():

lg \frac{F_{0} - F}{F} = lg K_{a} + n lg [Q]

where F 0 and F are the fluorescence intensity before and after addition of single enantiomer, respectively, and [ Q ] is the concentration of single enantiomer.…”

Section: Resultsmentioning

confidence: 78%

“…All the Kq data were larger than the maximum value of collision quenching constant (2.0 Â 10 10 l mol À1 s À1 ), which confirmed that the SA quenching processes were caused by static quenching mechanisms. 35 Thus, association constant (K a ) and the number of binding sites (n) can be obtained from the double-logarithm curve on the basis of the static quenching Equation (5): 36 lg…”

Section: Investigation Of the Interaction Between Serum Albumin And Ementioning

confidence: 99%

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A New Biosensor for Chiral Recognition Using Goat and Rabbit Serum Albumin Self‐Assembled Quartz Crystal Microbalance

Chen

Zhang

et al. 2012

Chirality

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Quartz crystal microbalance (QCM) biosensor was used for the chiral recognition of five pairs of enantiomers by using goat serum albumin (GSA) and rabbit serum albumin (RbSA) as chiral selectors. Serum albumin (SA) was immobilized on the QCM through the self-assembled monolayer technique, and the surface concentration of GSA and RbSA were 8.8 × 10(-12) mol cm(-2) and 1.2 × 10(-11) mol cm(-2) , respectively. The QCM biosensors showed excellent sensitivity and selectivity. Meanwhile, the chiral recognition of SA sensors was quite species dependent. There were differences between GSA and RbSA sensors in the ability and the preference of chiral recognition. To R,S-1,2,3,4-tetrahydro-1-naphthylamine (R,S-1-TNA), R,S-1-(4-methoxyphenyl)ethylamine (R,S-4-MPEA), and R,S-1-(3-methoxyphenyl)ethylamine (R,S-3-MPEA), the preference of the stereoselective SA-drug binding of the two kinds of SA sensors were consistent. However, to R,S-2-octanol (R, S-2-OT) and R,S-methyl lactate (R,S-MEL), the two kinds of SA sensors had opposite chiral recognition preference. Moreover, the interactions of SA and the five pairs of enantiomers have been further investigated through ultraviolet (UV) and fluorescent (FL) spectra. The UV/FL results were in accordance with the consequence of QCM.

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lg \frac{F_{0} - F}{F} = lg K_{a} + n lg [Q]

where F 0 and F are the fluorescence intensity before and after addition of single enantiomer, respectively, and [ Q ] is the concentration of single enantiomer.…”

Section: Resultsmentioning

confidence: 78%

Section: Investigation Of the Interaction Between Serum Albumin And Ementioning

confidence: 99%

A New Biosensor for Chiral Recognition Using Goat and Rabbit Serum Albumin Self‐Assembled Quartz Crystal Microbalance

Chen

Zhang

et al. 2012

Chirality

View full text Add to dashboard Cite

show abstract

“…For a protein having n equivalent binding sites, the binding process for the quencher Q has been represented by :

n Q + P \leftrightarrow Q_{n} P

and the binding equilibrium constant as

K = [Q_{n} P] / [P]_{free} {[Q]}_{free}^{n}

…”

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

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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.

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“…The comparatively large K A value indicates that there was a relatively strong interaction between derivatives and BSA. The binding constant between BSA and derivatives decreased with the increases of temperature and n was also inversely correlated with temperature, which suggests the bonds of BSA with derivatives were an exothermic reaction . The n values were close to 1, which implies that there was a single binding site between BSA and derivatives.…”

Section: Resultsmentioning

confidence: 99%

Synthesis and interaction of bovine serum albumin with p‐hydroxybenzoic acid derivatives

et al. 2012

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Three novel p-hydroxybenzoic acid derivatives (HSOP, HSOX, HSCP) were synthesized from p-hydroxybenzoic acid and sulfonamides (sulfamonomethoxine sodium, sulfamethoxazole and sulfachloropyridazine sodium) and characterized by elemental analysis, HNMR and MS. Interactions between derivatives and bovine serum albumin (BSA) were studied by fluorescence quenching spectra, UV-vis absorption spectra and time-resolved fluorescence spectra. Based on fluorescence quenching calculation and Förster's non-radioactive energy transfer theory, the values of the binding constants, basic thermodynamic parameters and binding distances were obtained. Experimental results indicated that the three derivatives had a strong ability to quench fluorescence from BSA and that the binding reactions of the derivatives with BSA were a static quenching process. Thermodynamic parameters showed that binding reactions were spontaneous and exothermic and hydrogen bond and van der Waals force were predominant intermolecular forces between the derivatives and BSA. Synchronous fluorescence spectra suggested that HSOX and HSCP had little effect on the microenvironment and conformation of BSA in the binding reactions but the microenvironments around tyrosine residues were disturbed and polarity around tyrosine residues increased in the presence of HSOP.

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Binding of several benzodiazepines to bovine serum albumin: Fluorescence study

Cited by 49 publications

References 20 publications

A New Biosensor for Chiral Recognition Using Goat and Rabbit Serum Albumin Self‐Assembled Quartz Crystal Microbalance

A New Biosensor for Chiral Recognition Using Goat and Rabbit Serum Albumin Self‐Assembled Quartz Crystal Microbalance

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

Synthesis and interaction of bovine serum albumin with p‐hydroxybenzoic acid derivatives

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