Photon Correlation Spectroscopy Investigations of Proteins

Gun'ko, V.М.; Klyueva, Alla V.; Levchuk, Yuri N.; Лебода, Р.

doi:10.1002/chin.200403280

Cited by 7 publications

(17 citation statements)

References 1 publication

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“…A similar type of the pH dependence of adsorption is characteristic for other systems in which interaction of proteins with a silica surface occurs predominantly due to electrostatic forces and hydrogen bonds (the main portion of which is due to electrostatic forces). A similar effect is observed for other plasma proteins interacting with nanosilica [4,27].…”

Section: Adsorption Of Hpfsupporting

confidence: 80%

“…The coagulation effects could be enhanced by interaction of HPF molecules with several primary silica particles simultaneously from the same or different aggregates that leaded to the formation of larger and denser hybrid HPF/silica aggregates and agglomerates. Similar effects were observed on interaction of different proteins with different nanosilicas [25,27,28,39]. The electronic reflection spectra of HPF adsorbed on silica (Fig.…”

Section: Adsorption Of Hpfsupporting

confidence: 73%

“…2d) calculated from the HPF adsorption data (Fig. 2a) and Langmuir equation as the kernel of the integral equation solved using the regularization procedure [27]. The graphs of ΔG(C uw ) for the majority of the studied systems have two portions (nearly linear sections) related to both strongly and weakly bound waters.…”

Section: Interfacial Water In Hpf and Hpf/nanosilica Solutionsmentioning

confidence: 98%

“…The adsorption slightly decreases (by ∼20% at pH 8) at pH > 6 (Fig. 2b) because the adsorption of proteins is maximal at their isoelectric point [27]. Consequently, the state of HPF is stable at pH 5-8 which is important because HPF can easily denature in strongly acid or base solutions as well as upon adsorption.…”

Section: Adsorption Of Hpfmentioning

confidence: 99%

“…However, this method has not been used to study the adsorption of HPF onto nanosilica. Our previous investigations of interactions of bovine serum albumin (BSA) and HSA, gelatin, RBCs, yeast cells, as well as different polymers, with nanosilica using 1 H NMR, FTIR, and UV/vis spectroscopies, thermally stimulated depolarization current (TSDC), adsorption and other methods [25][26][27][28][29] have shown that the state of interfacial water at the silica surface strongly changes upon adsorption of macromolecules or cells. Interaction of HPF with nanosilica is of special interest because of the medical applications of this material [3,4], especially as a component of tourniquet preparations.…”

Section: Introductionmentioning

confidence: 99%

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Interaction of fibrinogen with nanosilica

et al. 2007

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Interaction of human plasma fibrinogen (HPF) with fumed nanosilica A-300 in a phosphate buffer solution (PBS) was studied using 1 H NMR spectroscopy with layer-by-layer freezing-out of bulk and interfacial water in the temperature range of 210-273 K, TSDC (90 < T < 265 K), adsorption, FTIR, and UV spectroscopy methods. An increase in concentration of HPF in the PBS leads to a decrease in amounts of structured water (frozen at T < 273 K) because of coagulation of HPF molecules. Addition of nanosilica to the HPF solution strongly reduces the amounts of structured water because of adsorption interaction of HPF molecules with silica nanoparticles, self-association of HPF molecules, formation of denser packed hybrid agglomerates with HPF and silica, and lastly, because of conformational changes of HPF. A monolayer adsorption capacity of A-300 corresponds to 156 mg of HPF per gram of silica. The FTIR and UV spectra show that the HPF adsorption on silica leads to structural changes of the protein molecules. These changes and formation of hybrid HPF/A-300 aggregates can increase the rate of clotting that is of importance on nanosilica application as a component of tourniquet preparations.

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Section: Adsorption Of Hpfsupporting

confidence: 80%

Section: Adsorption Of Hpfsupporting

confidence: 73%

Section: Interfacial Water In Hpf and Hpf/nanosilica Solutionsmentioning

confidence: 98%

Section: Adsorption Of Hpfmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Interaction of fibrinogen with nanosilica

et al. 2007

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Protein aggregation: Pathways, induction factors and analysis

Mahler

Frieß

Grauschopf

et al. 2009

Journal of Pharmaceutical Sciences

764

635

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Dynamics of proteins in solution

Grimaldo

Roosen-Runge

Zhang

et al. 2019

Quart. Rev. Biophys.

107

164

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The dynamics of proteins in solution includes a variety of processes, such as backbone and side-chain fluctuations, interdomain motions, as well as global rotational and translational (i.e. center of mass) diffusion. Since protein dynamics is related to protein function and essential transport processes, a detailed mechanistic understanding and monitoring of protein dynamics in solution is highly desirable. The hierarchical character of protein dynamics requires experimental tools addressing a broad range of time- and length scales. We discuss how different techniques contribute to a comprehensive picture of protein dynamics, and focus in particular on results from neutron spectroscopy. We outline the underlying principles and review available instrumentation as well as related analysis frameworks.

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Photon Correlation Spectroscopy Investigations of Proteins

Cited by 7 publications

References 1 publication

Interaction of fibrinogen with nanosilica

Interaction of fibrinogen with nanosilica

Protein aggregation: Pathways, induction factors and analysis

Dynamics of proteins in solution

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