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Dynamic properties of the layers of cupin-1.1 aggregates at the air/water interface. / Исаков, Николай Анатольевич; Белоусов, Михаил Владимирович; Нижников, Антон Александрович; Носков, Борис Анатольевич.
в: Biophysical Chemistry, Том 307, 107166, 01.04.2024.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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TY - JOUR
T1 - Dynamic properties of the layers of cupin-1.1 aggregates at the air/water interface
AU - Исаков, Николай Анатольевич
AU - Белоусов, Михаил Владимирович
AU - Нижников, Антон Александрович
AU - Носков, Борис Анатольевич
PY - 2024/4/1
Y1 - 2024/4/1
N2 - Spread layers of amorphous aggregates of the structural domain of plant protein vicilin, cupin-1.1, at the water – air interface were studied by the surface tensiometry, dilational surface rheology, Brewster angle and atomic force microscopy. The layer properties differed strongly from the results for the layers of previously studied proteins. The dependency of the dynamic elasticity of the layer on surface pressure had two local maxima with the second peak being four times higher than the first one. In the region of the first maximum the obtained results are similar to those for dispersions of polymer microgels with a hairy corona. At the beginning of surface compression separate threads of the corona are stretched along the surface and the surface elasticity increases. The further compression results in the formation of loops and tails leading to a decrease of the elasticity. The second local maximum of the dynamic surface elasticity is presumably caused by the interactions of the rigid cores of the aggregates leading finally to the formation of multilayer structures at high surface pressures. In this case, the surface elasticity starts to decrease as a result of the segment exchange between different layers at the interface.
AB - Spread layers of amorphous aggregates of the structural domain of plant protein vicilin, cupin-1.1, at the water – air interface were studied by the surface tensiometry, dilational surface rheology, Brewster angle and atomic force microscopy. The layer properties differed strongly from the results for the layers of previously studied proteins. The dependency of the dynamic elasticity of the layer on surface pressure had two local maxima with the second peak being four times higher than the first one. In the region of the first maximum the obtained results are similar to those for dispersions of polymer microgels with a hairy corona. At the beginning of surface compression separate threads of the corona are stretched along the surface and the surface elasticity increases. The further compression results in the formation of loops and tails leading to a decrease of the elasticity. The second local maximum of the dynamic surface elasticity is presumably caused by the interactions of the rigid cores of the aggregates leading finally to the formation of multilayer structures at high surface pressures. In this case, the surface elasticity starts to decrease as a result of the segment exchange between different layers at the interface.
KW - Dilational surface rheology
KW - Plant proteins
KW - Protein aggregates
KW - Spread layers
KW - Surface pressure
UR - https://www.mendeley.com/catalogue/5df183b7-5cd8-36bf-9308-7cc4ca0dceba/
U2 - 10.1016/j.bpc.2023.107166
DO - 10.1016/j.bpc.2023.107166
M3 - Article
VL - 307
JO - Biophysical Chemistry
JF - Biophysical Chemistry
SN - 0301-4622
M1 - 107166
ER -
ID: 116018003