The effect of lead cations on the fluorescence characteristics of bovine serum albumin in aqueous solution

Sergeeva, I. A.; Shirshin, E. A.; Zhdanova, Nadezda G.; Gibizova, V. V.; Петрова, Г. П.; Kurguzenkov, S. A.; Фадеев, В. В.

doi:10.1134/s0030400x1308016x

Cited by 4 publications

(3 citation statements)

References 19 publications

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“…A vast number of biological applications of fluorescence anisotropy have been reported to date due to the comparable timescale of rotational diffusion of biopolymers and the fluorescence lifetime of many fluorophores. Anisotropy measurement can provide information on the shape and size of proteins and have been used to measure protein-protein associations, the fluidity of membranes, binding and conformational dynamics [ 34 , 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 , 43 ]. However, fluorescence anisotropy is highly dependent on the environment (solvent viscosity), the size and shape of the fluorophore and the flexibility of the protein [ 2 ].…”

Section: Tryptophan Fluorescencementioning

confidence: 99%

Intrinsic Tryptophan Fluorescence in the Detection and Analysis of Proteins: A Focus on Förster Resonance Energy Transfer Techniques

Ghisaidoobe

Chung

2014

IJMS

692

474

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Förster resonance energy transfer (FRET) occurs when the distance between a donor fluorophore and an acceptor is within 10 nm, and its application often necessitates fluorescent labeling of biological targets. However, covalent modification of biomolecules can inadvertently give rise to conformational and/or functional changes. This review describes the application of intrinsic protein fluorescence, predominantly derived from tryptophan (λEX ∼ 280 nm, λEM ∼ 350 nm), in protein-related research and mainly focuses on label-free FRET techniques. In terms of wavelength and intensity, tryptophan fluorescence is strongly influenced by its (or the protein’s) local environment, which, in addition to fluorescence quenching, has been applied to study protein conformational changes. Intrinsic Förster resonance energy transfer (iFRET), a recently developed technique, utilizes the intrinsic fluorescence of tryptophan in conjunction with target-specific fluorescent probes as FRET donors and acceptors, respectively, for real time detection of native proteins.

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Section: Tryptophan Fluorescencementioning

confidence: 99%

Intrinsic Tryptophan Fluorescence in the Detection and Analysis of Proteins: A Focus on Förster Resonance Energy Transfer Techniques

Ghisaidoobe

Chung

2014

IJMS

692

474

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“…The main physical mechanisms of toxic action of heavy metal ions are the formation of supramolecular structuresdipole protein clusters in solutions of various proteins and enzymes containing heavy metal ions 11,12 . Proteins in solution are polyelectrolytes and the main type of interaction between them is the Coulomb repulsion.…”

Section: Introductionmentioning

confidence: 99%

Quenching of photoexcited states of the proteins chromophores and introduced into the protein macromolecules fluorescent probes by heavy metal ions

2015

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We have studied the processes of quenching of photoexcited states of fluorescent probes and quenching of the fluorescence of the chromophores of human serum albumin (HSA) by heavy metal ions (HM): cations Tl + , Pb 2+ , Cu 2+ , Cd 2+ , and the anion of iodine (I -). We used the dye from xanthene series -eosin as a fluorescent probe. By quenching of the fluorescence of protein chromophores we found an influence of HM on the structure of proteins, resulting in a shift of the peak of the fluorescence of HSA tryptophanyl. This can be explained by proteins denaturation under the influence of heavy metals and penetration of water into the inner environment of HSA tryptophan. It was established that the constant of the quenching of the probe phosphorescence is much higher than the fluorescence, which is explained by significantly longer lifetime of the photoexcited states of fluorescent probes in the triplet state than in the singlet.

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“…An important property of serum albumin is binding and transport of different ligands: hormones, drugs, fatty acids, including metal ions [1][2][3][4] . Many heavy metals, such as iron, copper, zinc, molybdenum, are involved in biological processes and they are necessary micronutrients in the specified amounts.…”

Section: Introductionmentioning

confidence: 99%

Comparative studies of the effects of copper sulfate and zinc sulfate on serum albumins

Plotnikova

Мельников

Melnikov

et al. 2016

Saratov Fall Meeting 2015: Third International Symposium on Optics and Biophotonics and Seventh Finnish-Russian Photonics and L

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The work is devoted to the study of the interaction of heavy metals with bovine serum albumin (BSA) and human serum albumin (HSA), by quenching of the intrinsic fluorescence of proteins and fluorescent probe pyrene by heavy metal ions. Sulfates of copper and zinc (CuSO 4 , ZnSO 4 ) were taken as the metal salts. The value of the Stern-Volmer constants of quenching of intrinsic fluorescence of proteins and fluorescence probe pyrene reduced from Cu (II) to the Zn (II). It was experimentally found that the copper ions have a greater ability to fluorescence quenching, which is probably associated with the greater availability of protein chromophore groups to copper ions and with adsorbed fluorescent probe pyrene in the protein globule.

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The effect of lead cations on the fluorescence characteristics of bovine serum albumin in aqueous solution

Cited by 4 publications

References 19 publications

Intrinsic Tryptophan Fluorescence in the Detection and Analysis of Proteins: A Focus on Förster Resonance Energy Transfer Techniques

Intrinsic Tryptophan Fluorescence in the Detection and Analysis of Proteins: A Focus on Förster Resonance Energy Transfer Techniques

Quenching of photoexcited states of the proteins chromophores and introduced into the protein macromolecules fluorescent probes by heavy metal ions

Comparative studies of the effects of copper sulfate and zinc sulfate on serum albumins

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