Effects of Cu2+ on stability and composition of water soluble ternary polyacrylic acid-Cu2+-protein complexes against radiation damage

Mastafaev, M. I.; Sarac, A. Sezai̇; Erkol, A. Y.; Bayülken, Seval; Dinçer, Betül; Sezer, Esma

doi:10.1007/bf00342455

Cited by 6 publications

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“…Previously we described the formation of water-soluble and water-insoluble ternary polycomplexes of proteins with synthetic polyelectrolytes (PEs) in the presence of transient metal ions (Fe 3+ , Ba 2+ , Cu 2+ , etc. ). − Such PE−metal−protein polycomplexes (PMCs) were obtained by simple mixing of solutions of proteins, metal ions, and PEs in water at different pH values. This method consists of the use of small concentrations of metal additives, which promote the PE binding to protein molecule without causing any appreciable changes in the chemical structure of components.…”

Section: Introductionmentioning

confidence: 99%

Fluorescence Study of Cu²⁺-Induced Interaction between Albumin and Anionic Polyelectrolytes

Filenko¹,

Demchenko²,

Mustafaeva³

et al. 2000

Biomacromolecules

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The Cu(2+)-induced complex formation of bovine serum albumin (BSA) with anionic polyelectrolytes (PEs) (polyacrylic acid (PAA), poly(N-isopropylacrylamide) [poly[NIPAAm]], and copolymers of N-isopropylacrylamide (NIPAAm) and acrylic acid) in aqueous solution was studied by a fluorescence technique and high-performance liquid chromatography analysis. The character of the interactions depends on the monomer composition (r = [COOH]/[NIPAAm]), [Cu(2+)]/[PE], and [BSA]/[PE] ratios and solution pH. Two types of ternary polycomplex (polymer + Cu(2+) + BSA) particles are formed depending on the monomer composition r of the copolymer. At r from 1/3 to 1/1, the protein molecules in the structure of ternary polycomplex particles are densely covered by the shell of a polymer coil and practically "fenced off" from the water environment. At r > or = 3/1 ternary polycomplex PAA-Cu(2+)-BSA particles have more friable structures in which protein molecules are practically exposed to the solution. At low polymer concentration, an intrapolymer ternary polycomplex is formed. This complex aggregates to an interpolymer species upon increase in polymer concentration. Fluorescence data indicate that in ternary complex polymer interacts through Cu(2+) ions with BSA preferentially at the site close to the location of "cleft" tryptophan residue. This leads to static quenching of this tryptophan fluorescence. Cu(2+)-induced complex formation is an equilibrium reaction.

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Section: Introductionmentioning

confidence: 99%

Fluorescence Study of Cu²⁺-Induced Interaction between Albumin and Anionic Polyelectrolytes

Filenko¹,

Demchenko²,

Mustafaeva³

et al. 2000

Biomacromolecules

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Investigation of Ternary Complex Formations of Polyacrylic Acid with Bovine Serum Albumin in the Presence of Metal Ions by Fluorescence and Dynamic Light Scattering Measurements

2010

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In this paper, the complex formation of bovine serum albumin (BSA) and polyacrylic acid (PAA) in the presence metal ions at pH = 7 has been examined by using fluorescence and dynamic light scattering measurements. It has been observed that the most stable complexes of polyacrylic acid and bovine serum albumin have occurred in the presence of copper(II) ions. The other ions have the ability to form weak complexes between polyions and bovine serum albumin. To prior characterizing the interaction between bovine serum albumin and polyacrylic acid, the dynamic light scattering technique have been applied to determine the intensity-size distributions of the solutions of bovine serum albumin, polyacrylic acid, and ternary mixtures containing various molar ratios of bovine serum albumin to polyacrylic acid (the molar ratios of bovine serum albumin to polyacrylic acid has been taken equal to 0.5, 1.0, 1.5, 2.0 and 2.5) prepared at different molar ratios of copper(II) ions/acrylic acid unit. When the molar ratio of copper(II) ions to acrylic acid in the ternary mixtures has been lower than and equals to 0.3, two peaks have been observed in the curves of the intensity-size distributions due to contents of free bovine serum albumin and ternary complexes of polyacrylic acid-copper(II)-bovine serum albumin whereas when the molar ratio of copper(II) ions to acrylic acid equals to 0.4, the hydrodynamic diameter has pointed out only one peak. This result indicates that soluble and stable ternary complexes has occurred when the molar ratio of copper(II) ions to acrylic acid has been taken equal to 0.4.

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Radiation-induced formation of polyacrylic acid–protein covalent conjugates

Mustafaev

Bayülken²,

Ergen

et al. 2001

Radiation Physics and Chemistry

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Effects of Cu2+ on stability and composition of water soluble ternary polyacrylic acid-Cu2+-protein complexes against radiation damage

Cited by 6 publications

References 1 publication

Fluorescence Study of Cu²⁺-Induced Interaction between Albumin and Anionic Polyelectrolytes

Fluorescence Study of Cu²⁺-Induced Interaction between Albumin and Anionic Polyelectrolytes

Investigation of Ternary Complex Formations of Polyacrylic Acid with Bovine Serum Albumin in the Presence of Metal Ions by Fluorescence and Dynamic Light Scattering Measurements

Radiation-induced formation of polyacrylic acid–protein covalent conjugates

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Effects of Cu2+ on stability and composition of water soluble ternary polyacrylic acid-Cu2+-protein complexes against radiation damage

Cited by 6 publications

References 1 publication

Fluorescence Study of Cu2+-Induced Interaction between Albumin and Anionic Polyelectrolytes

Fluorescence Study of Cu2+-Induced Interaction between Albumin and Anionic Polyelectrolytes

Investigation of Ternary Complex Formations of Polyacrylic Acid with Bovine Serum Albumin in the Presence of Metal Ions by Fluorescence and Dynamic Light Scattering Measurements

Radiation-induced formation of polyacrylic acid–protein covalent conjugates

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Fluorescence Study of Cu²⁺-Induced Interaction between Albumin and Anionic Polyelectrolytes

Fluorescence Study of Cu²⁺-Induced Interaction between Albumin and Anionic Polyelectrolytes