Research output: Contribution to journal › Article › peer-review
Surface properties of recombinant pea vicilin and cupin-1.2 solutions in 8M urea. / Исаков, Николай Анатольевич; Ангел, Дмитрий Витальевич; Белоусов, Михаил Владимирович; Loglio, Giuseppe; Miller, Reinhard; Нижников, Антон Александрович; Носков, Борис Анатольевич.
In: Polymers, Vol. 17, No. 18, 2463, 11.09.2025.Research output: Contribution to journal › Article › peer-review
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TY - JOUR
T1 - Surface properties of recombinant pea vicilin and cupin-1.2 solutions in 8M urea
AU - Исаков, Николай Анатольевич
AU - Ангел, Дмитрий Витальевич
AU - Белоусов, Михаил Владимирович
AU - Loglio, Giuseppe
AU - Miller, Reinhard
AU - Нижников, Антон Александрович
AU - Носков, Борис Анатольевич
PY - 2025/9/11
Y1 - 2025/9/11
N2 - The kinetic dependencies of the surface pressure, the dilational dynamic surface elasticity and ellipsometric angles of cupin-1.2 and vicilin solutions in 8M urea were measured at different concentrations. The analysis of these kinetics dependencies and the obtained master curves allowed us to determine a few adsorption steps in the investigated systems and showed that the master curves are individual characteristics of the protein for a given solvent. At the same time, the shape of these curves can be different for adsorbed and spread layers of plant proteins indicating different structures of these layers. The dependencies of the dynamic surface elasticity on surface pressure are non-monotonic, unlike the corresponding results for most of the solutions of the investigated plant proteins. The extremums of these dependencies can be connected to the formation of the distal region of the surface layer in agreement with the theory for the surface viscoelasticity of polymer solutions.
AB - The kinetic dependencies of the surface pressure, the dilational dynamic surface elasticity and ellipsometric angles of cupin-1.2 and vicilin solutions in 8M urea were measured at different concentrations. The analysis of these kinetics dependencies and the obtained master curves allowed us to determine a few adsorption steps in the investigated systems and showed that the master curves are individual characteristics of the protein for a given solvent. At the same time, the shape of these curves can be different for adsorbed and spread layers of plant proteins indicating different structures of these layers. The dependencies of the dynamic surface elasticity on surface pressure are non-monotonic, unlike the corresponding results for most of the solutions of the investigated plant proteins. The extremums of these dependencies can be connected to the formation of the distal region of the surface layer in agreement with the theory for the surface viscoelasticity of polymer solutions.
UR - https://www.mdpi.com/2073-4360/17/18/2463
UR - https://www.mendeley.com/catalogue/09f10f68-de70-3b7f-a48c-4e5817ed8d85/
U2 - 10.3390/polym17182463
DO - 10.3390/polym17182463
M3 - Article
C2 - 41012227
VL - 17
JO - Polymers
JF - Polymers
SN - 2073-4360
IS - 18
M1 - 2463
ER -
ID: 140750228