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| 001 | 1017753 | ||
| 005 | 20231215102632.0 | ||
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| 100 | 1 | _ | |a Kang, Kyongok |0 P:(DE-Juel1)130749 |b 0 |e Corresponding author |
| 245 | _ | _ | |a The effect of fatty acids, ionic strength, and electric fields on the microscopic dynamics of BSA aggregates |
| 260 | _ | _ | |a Lausanne |c 2023 |b Frontiers Media |
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| 520 | _ | _ | |a This paper presents the microscopic dynamics of the concentrated suspensions ofbovine serum albumin (BSA) proteins and their aggregates by dynamic lightscattering (DLS) experiments. The effects of fatty acids binding to BSA, as wellas the ionic strength and weak electric field, are discussed for affecting the stabilityof BSA suspensions against calcium-induced aggregation. By variation of the ionicstrength, in the absence of an external electric field, DLS experiments show thatmonomer–BSA interactions (in the essentially fatty acid-free case) are overallrepulsive but that, nevertheless, aggregation occurs to some extent. Also, thediffusive properties of different types of BSA are explored under an applied low-ACelectric field by means of in situ electric small-angle depolarized DLS experiments,which reveal a significant decrease of the translational BSA–monomer diffusioncoefficient with increasing frequency, while the aggregates indicate orientationalmotion via rotation on applying an electric field. These observations areinterpreted in terms of (localized) orientation interactions obtained asoscillations in the intermediate scattering correlation function, as well as theanomalous slower relaxations as resulting in effective (collective) dynamicsbetween monomeric BSA and their protein aggregates. |
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| 773 | _ | _ | |a 10.3389/fphy.2023.1282099 |g Vol. 11, p. 1282099 |0 PERI:(DE-600)2721033-9 |p 1282099 |t Frontiers in physics |v 11 |y 2023 |x 2296-424X |
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