TY - JOUR

T1 - Dynamic Surface Properties of α-lactalbumin Fibril Dispersions

AU - Носков, Борис Анатольевич

AU - Loglio, Giuseppe

AU - Miller, Reinhard

AU - Миляева, Ольга Юрьевна

AU - Панаева, Мария Александровна

AU - Быков, Алексей Геннадьевич

PY - 2023/10/2

Y1 - 2023/10/2

N2 - The dynamic surface properties of aqueous dispersions of α-lactalbumin (ALA) amyloid fibrils differ noticeably from the properties of the fibril dispersions of other globular proteins. As a result, the protocol of the application of ALA fibrils to form stable foams and emulsions has to be deviate from that of other protein fibrils. Unlike the fibrils of β-lactoglobulin and lysozyme, ALA fibrils can be easily purified from hydrolyzed peptides and native protein molecules. The application of the oscillating barrier method shows that the dynamic surface elasticity of ALA fibril dispersions exceeds the surface elasticity of native protein solutions at pH 2. ALA fibrils proved to be stable at this pH, but the stability breaks at higher pH levels when the fibrils start to release small peptides of high surface activity. As a result, the dynamic surface properties of ALA coincide with those of native protein solutions. The ionic strength strongly influences the adsorption kinetics of both fibril dispersions and native protein solutions but have almost no impact on the structure of the adsorption layers.

AB - The dynamic surface properties of aqueous dispersions of α-lactalbumin (ALA) amyloid fibrils differ noticeably from the properties of the fibril dispersions of other globular proteins. As a result, the protocol of the application of ALA fibrils to form stable foams and emulsions has to be deviate from that of other protein fibrils. Unlike the fibrils of β-lactoglobulin and lysozyme, ALA fibrils can be easily purified from hydrolyzed peptides and native protein molecules. The application of the oscillating barrier method shows that the dynamic surface elasticity of ALA fibril dispersions exceeds the surface elasticity of native protein solutions at pH 2. ALA fibrils proved to be stable at this pH, but the stability breaks at higher pH levels when the fibrils start to release small peptides of high surface activity. As a result, the dynamic surface properties of ALA coincide with those of native protein solutions. The ionic strength strongly influences the adsorption kinetics of both fibril dispersions and native protein solutions but have almost no impact on the structure of the adsorption layers.

KW - amyloid fibrils

KW - molten globules

KW - stability of fibril dispersions

KW - surface dilational elasticity

KW - surface pressure

KW - α-lactalbumin

UR - https://www.mendeley.com/catalogue/9b8d1ff8-d971-305c-8a16-337b846f9fc4/

U2 - 10.3390/polym15193970

DO - 10.3390/polym15193970

M3 - Article

C2 - 37836019

VL - 15

JO - Polymers

JF - Polymers

SN - 2073-4360

IS - 19

M1 - 3970

ER -