Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
Impact of denaturing agents on surface properties of myoglobin solutions. / Krycki, Michael M.; Lin, Shi Yow; Loglio, Giuseppe; Michailov, Alexander V.; Miller, Reinhard; Noskov, Boris A.
в: Colloids and Surfaces B: Biointerfaces, Том 202, 111657, 01.06.2021.Результаты исследований: Научные публикации в периодических изданиях › статья › Рецензирование
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TY - JOUR
T1 - Impact of denaturing agents on surface properties of myoglobin solutions
AU - Krycki, Michael M.
AU - Lin, Shi Yow
AU - Loglio, Giuseppe
AU - Michailov, Alexander V.
AU - Miller, Reinhard
AU - Noskov, Boris A.
N1 - Funding Information: This work was supported by the Russian Foundation of Basic Research, and the Ministry of Science and Technology of Taiwan (joint project no. 19-53-52006). The authors are also grateful to the Centre for Optical and Laser Materials Research of SPbU and to the Chemical Analysis and Materials Research Centre of SPbU for the use of their equipment. Publisher Copyright: © 2021 Elsevier B.V.
PY - 2021/6/1
Y1 - 2021/6/1
N2 - The addition of denaturants strongly influences the surface properties of aqueous myoglobin solutions. The effect differs from the results for mixed solutions of the denaturants and other globular proteins, for example, bovine serum albumin (BSA), lysozyme and β-lactoglobulin (BLG), although the surface properties of the solutions of the pure proteins are similar. The kinetic dependencies of the dynamic surface elasticity of myoglobin solutions with guanidine hydrochloride (GuHCl) reveal at least two adsorption steps at denaturant concentrations higher than 1 M: a very fast increase of the dynamic surface elasticity to approximately 30 mN/m at the beginning of adsorption, and a slower growth to abnormally high values of 250–300 mN/m. At the same time, the surface elasticity of BSA/GuHCl, BLG/GuHCl and lysozyme/GuHCl solutions is a non-monotonic function of the surface age, and does not exceed 50 mN/m close to equilibrium. The high surface elasticity of myoglobin/GuHCl solutions may be associated with protein aggregation in the surface layer. The formation of aggregates is confirmed by ellipsometry and Brewster angle microscopy. The addition of ionic surfactants to protein solutions leads to the formation of myoglobin/surfactant complexes, and the kinetic dependencies of the dynamic surface elasticity display local maxima indicating multistep adsorption kinetics, unlike the corresponding results for solutions of other globular proteins mixed with ionic surfactants. Ellipsometry and infrared reflection-absorption spectroscopy allow tracing the adsorption of the complexes and their displacement from the interface at high surfactant concentrations.
AB - The addition of denaturants strongly influences the surface properties of aqueous myoglobin solutions. The effect differs from the results for mixed solutions of the denaturants and other globular proteins, for example, bovine serum albumin (BSA), lysozyme and β-lactoglobulin (BLG), although the surface properties of the solutions of the pure proteins are similar. The kinetic dependencies of the dynamic surface elasticity of myoglobin solutions with guanidine hydrochloride (GuHCl) reveal at least two adsorption steps at denaturant concentrations higher than 1 M: a very fast increase of the dynamic surface elasticity to approximately 30 mN/m at the beginning of adsorption, and a slower growth to abnormally high values of 250–300 mN/m. At the same time, the surface elasticity of BSA/GuHCl, BLG/GuHCl and lysozyme/GuHCl solutions is a non-monotonic function of the surface age, and does not exceed 50 mN/m close to equilibrium. The high surface elasticity of myoglobin/GuHCl solutions may be associated with protein aggregation in the surface layer. The formation of aggregates is confirmed by ellipsometry and Brewster angle microscopy. The addition of ionic surfactants to protein solutions leads to the formation of myoglobin/surfactant complexes, and the kinetic dependencies of the dynamic surface elasticity display local maxima indicating multistep adsorption kinetics, unlike the corresponding results for solutions of other globular proteins mixed with ionic surfactants. Ellipsometry and infrared reflection-absorption spectroscopy allow tracing the adsorption of the complexes and their displacement from the interface at high surfactant concentrations.
KW - Chaotropic denaturants
KW - Dilational surface rheology
KW - Myoglobin
KW - Protein adsorption
KW - Protein denaturation
KW - Surfactants
KW - Surface-Active Agents
KW - Adsorption
KW - Solutions
KW - Rheology
KW - Surface Properties
KW - Elasticity
KW - AIR/WATER INTERFACE
KW - HEMOGLOBIN
KW - DODECYL-SULFATE
KW - AIR-WATER-INTERFACE
KW - PROTEIN/SURFACTANT ADSORPTION LAYER
KW - LYSOZYME
KW - PHOSPHATE BUFFER
KW - PH
KW - PROTEINS
KW - GEMINI SURFACTANTS
UR - http://www.scopus.com/inward/record.url?scp=85102146628&partnerID=8YFLogxK
UR - https://www.mendeley.com/catalogue/5ae2e586-48e5-3a44-8dbb-66d4dad5837e/
U2 - 10.1016/j.colsurfb.2021.111657
DO - 10.1016/j.colsurfb.2021.111657
M3 - Article
C2 - 33684687
AN - SCOPUS:85102146628
VL - 202
JO - Colloids and Surfaces B: Biointerfaces
JF - Colloids and Surfaces B: Biointerfaces
SN - 0927-7765
M1 - 111657
ER -
ID: 86107110