Piezoelectric Quartz Crystal Impedance Study of the Pb2+-induced Precipitation of Bovine Serum Albumin and Its Dissolution with EDTA in an Aqueous Solution

Yu, Yuan; Cai, Yan; Xie, Qingji; Yao, Shouzhuo

doi:10.2116/analsci.18.767

Cited by 9 publications

(5 citation statements)

References 34 publications

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“…For a pure albumin solution, a strong fluorescence signal is visible for the excitation wavelength from 275 nm to 295 nm. This strong fluorescence signal mostly comes from two aromatic residues of tyrosine (Tyr) and tryptophan (Trp) located in subdomain IIIA and 214th residue of subdomain IIA, respectively [22]. The only other feature of this spectrum is due to a weak Raman signal from water molecules at around 3400 cm −1 with respect to the excitation wavelength.…”

Section: Resultsmentioning

confidence: 99%

“…These binding sites enable the molecule to regulate intercellular metabolic fluxes and interactions with pharmaceuticals. Thus, the ability of serum albumins to bind lead ions is well known, and has been used to detect micromolar concentrations of lead ions in solution [22, 23]. In this report we illustrate a method which not only increases the sensitivity of detection by several orders of magnitude but also demonstrates the physiological changes in albumin due to the interaction with lead.…”

Section: Introductionmentioning

confidence: 92%

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Structural changes of human serum albumin in response to a low concentration of heavy ions

Saha

Yakovlev

2010

Journal of Biophotonics

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Lead ions in solution interact strongly with human serum albumin and modify the properties and function of albumin molecules. In the present study, we used optical spectroscopic techniques to explore the binding sites of lead, present in albumin. Structural and chemical analysis of albumin molecules using fluorescence and Raman spectroscopy, predicted the modification of two major amino acids in albumin due to lead binding. No secondary structural changes are observed in the protein molecule, which is further confirmed using circular dichroism absorption measurements. The results indicate that loss of charge from the binding site of albumin by the charged lead ions, give rise to dipole interaction which acts as the major contributor to promote protein agglomeration. Stepwise formation of a protein cluster in the presence of a lead ion.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 92%

Structural changes of human serum albumin in response to a low concentration of heavy ions

Saha

Yakovlev

2010

Journal of Biophotonics

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“…7,8 The ability of serum albumins to bind lead ions is well known, and has been used to detect micromolar concentrations of lead ions in solution. 9,10 In this report we demonstrate how the sensitivity of this detection can be increased by several orders of magnitude reaching an important level of picomolar concentrations. To achieve this goal, we take advantage of the excitation emission matrix ͑EEM͒ method for fluorescence detection, which has been proven to be a valuable method for multicomponent analysis.…”

mentioning

confidence: 64%

“…18 The only thiol group present in albumin is associated with Cys 34, which is present in domain I of HSA. 9 The nearest Tyr, Tyr 84, which surrounds the sulfur of Cys 34, gets affected due to the binding of lead ion with Cys. 16 Fluorescence spectra for excitation at 275 nm, which corresponds to Tyr show a gradual decrease with an increase in concentration of lead ions ͓Fig.…”

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confidence: 99%

Detection of picomolar concentrations of lead in water using albumin-based fluorescence sensor

Saha

Yakovlev

2009

Applied Physics Letters

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Comprehensive analysis of fluorescence of albumin shows a weak fluorescence band at 430 nm, whose intensity exhibits a remarkable sensitivity to the presence of heavy ions in water. Using this fluorescence as a marker, as low as 10 pM concentration of lead can be routinely detected. Such a great sensitivity is explained in terms of electrostatic interactions in solution, which promote protein agglomeration. The latter is independently confirmed using dynamic light scattering measurements. © 2009 American Institute of Physics. ͓doi:10.1063/1.3246792͔Heavy metals, such as lead, mercury, cadmium, and arsenic, present a major threat to human health and society. In particular, lead is a commonly occurring environmental hazard, which is widely recognized to be toxic at concentrations as low as 1 pM. 1,2 While environmental efforts have resulted in significant reduction in lead exhaust into the biosphere, a considerable amount of lead is still present in soil and leadbased paints, posing a danger to the society. Although the Environmental Protection Agency limits the allowable level of lead in drinking water to 15 ppb ͑73 nM͒, recent studies show that there is no threshold for the adverse effect of this universal toxic metal, which tends to substitute biological reactions mediated by calcium, iron, and other metal ions and enzymes. 1,3 This leads to lead poisoning resulting in serious medical conditions affecting brain development, and the cardiovascular and reproductive systems. 3 The deleterious effects of lead to human health and environment present an open challenge to the scientific community to develop sensors which can detect, monitor, and measure the presence of those toxic metals. 4,5 Several methods are currently available for detecting heavy metal ions. It includes atomic absorption spectrometry, inductively coupled plasma ͑ICP͒ atomic emission spectroscopy, and ICP mass spectrometry. 6 However, most of these techniques are either outrageously expensive or not sensitive enough in detecting the presence of toxic metals below nanomolar concentrations.In search for an alternative strategy to detect the heavy ions in solution, we evaluated the natural transport path of those ions in a human body. The most common media for transporting heavy metal ions is blood, most probably through binding to serum albumin, which is one of the most abundant proteins in blood serum, and which is also responsible for transport function. 7,8 The ability of serum albumins to bind lead ions is well known, and has been used to detect micromolar concentrations of lead ions in solution. 9,10 In this report we demonstrate how the sensitivity of this detection can be increased by several orders of magnitude reaching an important level of picomolar concentrations. To achieve this goal, we take advantage of the excitation emission matrix ͑EEM͒ method for fluorescence detection, which has been proven to be a valuable method for multicomponent analysis. 11 The EEM method helps to point out the excitation wavelength where there are primary ch...

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“…QCM can detect a mass change in the nanogram-order range according to Sauerbrey’s equation [ 20 ], which is used to analyze the adsorption phenomena on the QCO such as oxidation/reduction reaction, metal ion binding to Langmuir monolayer, and molecular recognition of DNA strands and lipids [ 21 , 22 , 23 , 24 , 25 , 26 ]. QCI can also detect and estimate a change in viscosity and elasticity of adsorbed organic and inorganic layers on the QCO independent of adsorbed mass [ 27 ] and be used in the analysis of changes in properties of adsorbed layers on the QCO such as hybridization of DNA [ 28 ], phase transition of Langmuir–Blodgett film [ 29 ], and protein precipitation denaturation [ 30 , 31 ]. It is expected that the use of QCM and QCI methods would help the elucidation of our targeted anesthesia phenomenon.…”

Section: Introductionmentioning

confidence: 99%

The Interaction between Anesthetic Isoflurane and Model-Biomembrane Monolayer Using Simultaneous Quartz Crystal Microbalance (QCM) and Quartz Crystal Impedance (QCI) Methods

Yamamoto,

Ito,

Akatsuka

et al. 2024

Membranes

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The interaction between anesthetic Isoflurane (Iso) and model-biomembrane on the water surface has been investigated using quartz crystal microbalance (QCM) and quartz crystal impedance (QCI) methods. The model-biomembranes used were dipalmitoyl phosphatidyl choline (DPPC), DPPC-palmitic acid (PA) mixture (DPPC:PA = 8:2), DPPC-Alamethicin (Al) mixture (DPPC:Al = 39:1), and DPPC-β-Lactoglobulin (βLG) mixture (DPPC:βLG = 139:1) monolayers, respectively. The quartz crystal oscillator (QCO) was attached horizontally to each monolayer, and QCM and QCI measurements were performed simultaneously. It was found that Iso hydrate physisorbed on each monolayer/water interface from QCM and changed those interfacial viscosities from QCI. With an increase in Iso concentration, pure DPPC, DPPC-PA mixed, and DPPC-Al mixed monolayers showed a two-step process of Iso hydrate on both physisorption and viscosity, whereas it was a one-step for the DPPC-βLG mixed monolayer. The viscosity change in the DPPC-βLG mixed monolayer with the physisorption of Iso hydrate was much larger than that of other monolayers, in spite of the one-step process. From these results, the action mechanism of anesthetics and their relevance to the expression of anesthesia were discussed, based on the “release of interfacial hydrated water” hypothesis on the membrane/water interface.

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Piezoelectric Quartz Crystal Impedance Study of the Pb2+-induced Precipitation of Bovine Serum Albumin and Its Dissolution with EDTA in an Aqueous Solution

Cited by 9 publications

References 34 publications

Structural changes of human serum albumin in response to a low concentration of heavy ions

Structural changes of human serum albumin in response to a low concentration of heavy ions

Detection of picomolar concentrations of lead in water using albumin-based fluorescence sensor

The Interaction between Anesthetic Isoflurane and Model-Biomembrane Monolayer Using Simultaneous Quartz Crystal Microbalance (QCM) and Quartz Crystal Impedance (QCI) Methods

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