Investigation of albumin-fullerenol interaction using laser correlation spectroscopy: the algorithm

Nepomnyashchaya, Elina; Savchenko, Ekaterina; Velichko, Elena; Aksenov, E. T.

doi:10.18287/jbpe16.02.040309

Cited by 4 publications

(2 citation statements)

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“…Such biological liquids as blood serum and plasma, saliva, solutions of complement proteins, albumin, thrombin, various amino acids and also magnetic liquids were investigated [5]. Polydisperse size distributions of nanoparticles in the biological fluids were obtained.…”

Section: Methodsmentioning

confidence: 99%

Modifications of laser correlation spectrometer for investigation of biological fluids

et al. 2017

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Abstract. We suggest three modifications of a laser correlation spectrometer for analysis of complex multicomponent biological solutions based on: (i) dynamic light scattering with special signal processing for analysis of polydisperse solutions, (ii) use of polarimetric technique for shape analysis, (iii) cross-correlation processing. The schemes of the devices based on polarization and cross-correlation analysis are described.

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Section: Methodsmentioning

confidence: 99%

Modifications of laser correlation spectrometer for investigation of biological fluids

et al. 2017

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“…The studies have demonstrated that they have clinical applications as carriers to transport drugs across the brain and ocular barriers [ 18 ]. In the work of Nepomnyashchaya et al, it is also shown that fullerenol can be used as a probing substance for the analysis of structural changes in proteins [ 19 ].…”

Section: Introductionmentioning

confidence: 99%

Quenching of Protein Fluorescence by Fullerenol C60(OH)36 Nanoparticles

Lichota

Szabelski

Krokosz

2022

IJMS

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The effect of the interaction between fullerenol C60(OH)36 (FUL) and alcohol dehydrogenase (ADH) from Saccharomyces cerevisiae and human serum albumin (HSA) was studied by absorption spectroscopy, fluorescence spectroscopy, and time-resolved fluorescence spectroscopy. As shown in the study, the fluorescence intensities of ADH and HSA at excitation wavelengths λex = 280 nm (Trp, Tyr) and λex = 295 nm (Trp) are decreased with the increase in the FUL concentration. The results of time-resolved measurements indicate that both quenching mechanisms, dynamic and static, are present. The binding constant Kb and the number of binding sites were obtained for HSA and ADH. Thus, the results indicated the formation of FUL complexes and proteins. However, the binding of FUL to HSA is much stronger than that of ADH. The transfer of energy from the protein to FUL was also proved.

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Light scattering in albumin solution under the influence of electric field in the regime of total internal reflection

Savchenko

Velichko

Aksenov

et al. 2018

J. Phys.: Conf. Ser.

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Investigation of albumin-fullerenol interaction using laser correlation spectroscopy: the algorithm

Cited by 4 publications

References 5 publications

Modifications of laser correlation spectrometer for investigation of biological fluids

Modifications of laser correlation spectrometer for investigation of biological fluids

Quenching of Protein Fluorescence by Fullerenol C60(OH)36 Nanoparticles

Light scattering in albumin solution under the influence of electric field in the regime of total internal reflection

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