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 -