Light scattering studies of the binding of bovine serum albumin to a cationic polyelectrolyte

Li, Yingjie; Mattison, Kevin; Dubin, Paul L.; Havel, Henry A.; Edwards, Shun L.

doi:10.1002/(sici)1097-0282(199604)38:4<527::aid-bip8>3.0.co;2-v

Cited by 52 publications

(50 citation statements)

References 43 publications

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“…[14][15][16][17][18] Depending upon such variables as pH, ionic strength (I), and the stoichiometry of polymer and protein concentrations, complexes may take the form of intrapolymerbound proteins, soluble aggregates, and coacervates or precipitates. Soluble complexes have been of particular interest to us for several reasons.…”

Section: Introductionmentioning

confidence: 59%

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Capillary Electrophoresis and Dynamic Light Scattering Studies of Structure and Binding Characteristics of Protein−Polyelectrolyte Complexes

1998

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Complex formation between sodium polystyrenesulfonate (NaPSS) and two proteins, bovine serum albumin and -lactoglobulin, was studied by dynamic light scattering (DLS) and capillary electrophoresis (CE) over a range of polyelectrolyte molecular weights. We found that the dimensions of the polyelectrolyte chain do not appear to change significantly upon complex formation and that the dependence of complex mobility on its composition is in agreement with a free-draining model. Estimates of intrinsic binding constants, sizes of binding site, and cooperativities in complex formation were obtained by fitting experimental data to the "overlapping binding sites" model. It was found that the cooperativities shown by the binding isotherms are consistent with the dependence of binding density upon NaPSS molecular weights. The latter can be predicted by the overlapping binding sites model for known binding cooperativity, but was not observed experimentally before.

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Section: Introductionmentioning

confidence: 59%

“…The binding of protein to polyelectrolyte may exhibit cooperativity, 17 which can be identified by analysis of binding † Current address: Parke-Davis Pharmaceutical Research, 2800 Plymouth Rd., Ann Arbor, MI 48105.…”

Section: Introductionmentioning

confidence: 99%

Capillary Electrophoresis and Dynamic Light Scattering Studies of Structure and Binding Characteristics of Protein−Polyelectrolyte Complexes

1998

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“…In the first part of the titration the Mü tek signal was the average of free HA and polyDADMAC-HA complex. Li et al (1996) have observed a similar behavior for the bovine serum albuminpolyDADMAC system.…”

Section: Mütek Particle Charge Detectormentioning

confidence: 92%

Humic substance charge determination by titration with a flexible cationic polyelectrolyte

Tan

Norde

Koopal

2011

Geochimica et Cosmochimica Acta

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“…On the other hand, at phase separation, I ) 0.10 M, pH φ ) 4.20 (point e), this domain is expanded and intensified, as expected, since phase separation requires that the number of bound proteins multiplied by their mean (negative) charge be sufficient to neutralize the charge on the polycation. 30 These models show that domain A at x ) 5 Å satisfies both criteria for determining a preferential region of binding: similarity at pH c values, and diminution at noninteraction conditions.…”

Section: M Are Confirmed By Dls As Shown Inmentioning

confidence: 99%

Identification by Integrated Computer Modeling and Light Scattering Studies of an Electrostatic Serum Albumin-Hyaluronic Acid Binding Site

et al. 2001

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Dynamic light scattering and turbidimetry, carried out on solutions of hyaluronic acid (HA) and bovine or human serum albumin (SA) at fixed ionic strength (I), revealed a critical pH corresponding to the onset of HA-SA soluble complex formation. Subsequent reduction of pH below pH c , corresponding to an increase in protein net positive charge, results in phase separation of the complex. The sensitivity of pH c to I indicated the primacy of electrostatic interactions in this process. Since pH c was always above the pK a of HA, these effects could be attributed to the influence of protein charge. The electrostatic potential around HSA was modeled using DelPhi (MSI) under pH, I conditions corresponding to incipient binding, phase separation, and noninteraction. At all incipient binding conditions (i.e., pH c , at varying I), an identical region of positive potential 5 Å from the protein van der Waals surface appeared. This unique domain intensified with a decrease in pH or I (corresponding to stronger binding), and diminished with an increase in pH or I (i.e., at noninteracting conditions). The size and low curvature of this domain could readily accommodate a 12 nm (decamer) sequence of HA. Simple electrostatic considerations indicate an electrostatic binding energy for the formation of this complex of ca. 1 kT, consistent with the condition of incipient complex formation. We suggest that such weak electrostatic binding may characterize nonspecific interactions for other proteingylcosaminoglycan pairs.

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Light scattering studies of the binding of bovine serum albumin to a cationic polyelectrolyte

Cited by 52 publications

References 43 publications

Capillary Electrophoresis and Dynamic Light Scattering Studies of Structure and Binding Characteristics of Protein−Polyelectrolyte Complexes

Capillary Electrophoresis and Dynamic Light Scattering Studies of Structure and Binding Characteristics of Protein−Polyelectrolyte Complexes

Humic substance charge determination by titration with a flexible cationic polyelectrolyte

Identification by Integrated Computer Modeling and Light Scattering Studies of an Electrostatic Serum Albumin-Hyaluronic Acid Binding Site

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