TY - JOUR

T1 - A comparison of surface properties for bovine serum albumin and human serum albumin – Dynamic/equilibrium surface tension and dilational modulus

AU - Tran, Van Nho

AU - Rivas, Johann Eduardo Maradiaga

AU - Hussain, Siam

AU - Tseng, Wen-Chi

AU - Акентьев, Александр Владимирович

AU - Носков, Борис Анатольевич

AU - Loglio, Giuseppe

AU - Lin, Shi-Yow

PY - 2023/12/1

Y1 - 2023/12/1

N2 - The biological functionalities of Human Serum Albumin (HSA) and Bovine Serum Albumin (BSA) have been extensively studied in the literature. However, limited information is available on their surface properties [dynamic/equilibrium surface tension (ST) and dilational modulus (E)]. This study compared the dynamic/equilibrium ST of HSA and BSA solutions and the E of the adsorbed films. A pendant bubble tensiometer was employed for measuring the relaxations of ST of HSA/BSA solutions at C = 0.01 – 90 (10−10 mol/cm3). The data revealed that while the dynamic ST of HSA(aq) and BSA(aq) exhibited a similar relaxation in general, the ST of HSA(aq) relaxed notably faster at the post-induction regime than BSA(aq). The equilibrium ST of both HSA and BSA was constant at 52.6 and 52.3 mN/m over a wide concentration range, C = 0.01 – 90 (10−10 mol/cm3). The E of HSA and BSA films exhibited a near-identical concentration dependency to each other: E was reasonably constant at ∼ 21 mN/m from C = 0.05 to 0.2 (10−10 mol/cm3), and at further concentration elevations, E rose notably, and eventually leveled off at ∼ 52 and ∼ 45 mN/m for HSA and BSA films, respectively.

AB - The biological functionalities of Human Serum Albumin (HSA) and Bovine Serum Albumin (BSA) have been extensively studied in the literature. However, limited information is available on their surface properties [dynamic/equilibrium surface tension (ST) and dilational modulus (E)]. This study compared the dynamic/equilibrium ST of HSA and BSA solutions and the E of the adsorbed films. A pendant bubble tensiometer was employed for measuring the relaxations of ST of HSA/BSA solutions at C = 0.01 – 90 (10−10 mol/cm3). The data revealed that while the dynamic ST of HSA(aq) and BSA(aq) exhibited a similar relaxation in general, the ST of HSA(aq) relaxed notably faster at the post-induction regime than BSA(aq). The equilibrium ST of both HSA and BSA was constant at 52.6 and 52.3 mN/m over a wide concentration range, C = 0.01 – 90 (10−10 mol/cm3). The E of HSA and BSA films exhibited a near-identical concentration dependency to each other: E was reasonably constant at ∼ 21 mN/m from C = 0.05 to 0.2 (10−10 mol/cm3), and at further concentration elevations, E rose notably, and eventually leveled off at ∼ 52 and ∼ 45 mN/m for HSA and BSA films, respectively.

KW - Bovine serum albumin

KW - Dilational modulus

KW - Dynamic surface tension

KW - Equilibrium surface tension

KW - Globular protein

KW - Human serum albumin

UR - https://www.mendeley.com/catalogue/bd3fd76c-1aff-3020-8a96-313feb8dcf81/

U2 - 10.1016/j.molliq.2023.123285

DO - 10.1016/j.molliq.2023.123285

M3 - Article

VL - 391

JO - Journal of Molecular Liquids

JF - Journal of Molecular Liquids

SN - 0167-7322

M1 - 123285

ER -