Bovine β-lactoglobulin (LGB) is a transport protein that can bind to its structure hydrophobic bioactive molecules. Due to the lack of toxicity, high stability and pH-dependent molecular binding mechanism, lactoglobulin can be used as a carrier of sparingly soluble drugs. Dynamic light scattering has confirmed LGB's tendency to create oligomeric forms. The hydrodynamic diameter of LGB molecules varies from 4 nm to 6 nm in the pH range of 2–10 and ionic strength I = 0.001–0.15 M, which corresponds to the presence of mono or dimeric LGB forms. The LGB zeta potential varies from 26.5 mV to −33.3 mV for I = 0.01 M and from 13.3 mV to −16 mV for I = 0.15 M in the pH range of 2–10. The isoelectric point is at pH 4.8. As a result of strong surface charge compensation, the maximum effective ionization degree of the LGB molecule is 35% for ionic strength I = 0.01 M and 22% for I = 0.15 M. The effectiveness of adsorption is linked with the properties of the protein, as well as those of the adsorption surface. The functionalization of gold surfaces with β-lactoglobulin (LGB) was studied using a quartz crystal microbalance with energy dissipation monitoring (QCM-D). The effectiveness of LGB adsorption correlates strongly with a charge of gold surface and the zeta potential of the molecule. The greatest value of the adsorbed mass was observed in the pH range in which LGB has a positive zeta potential values, below pH 4.8. This observation shows that electrostatic interactions play a dominant role in LGB adsorption on gold surfaces. Based on the adsorbed mass, protein orientation on gold surfaces was determined. The preferential side-on orientation of LGB molecules observed in the adsorption layer is consistent with the direction of the molecule dipole momentum determined by molecular dynamics simulations of the protein (MD). The use of the QCM-D method also allowed us to determine the effectiveness of adsorption of LGB on gold surface. Knowing the mechanism of LGB adsorption is significant importance for determining the optimum conditions for immobilizing this protein on solid surfaces. As β-lactoglobulin is a protein that binds various ligands, the binding properties of immobilized β-lactoglobulin can be used to design controlled protein structures for biomedical applications.

牛β-乳球蛋白（LGB）是一种转运蛋白，可以与其结构疏水生物活性分子结合。由于缺乏毒性，高稳定性和pH依赖性分子结合机制，乳球蛋白可以用作微溶性药物的载体。动态光散射已证实LGB有产生低聚形式的趋势。在2-10的pH范围内，LGB分子的流体动力学直径在4 nm至6 nm之间变化，离子强度I  = 0.001-0.15 M，这对应于LGB单体形式或二聚体形式的存在。用于LGBζ电位变化从26.5 mV至-33.3 mV的我 = 0.01 M和从13.3 mV至-16毫伏我 在2-10的pH范围内= 0.15M。等电点为pH 4.8。由于强的表面电荷补偿结果，LGB分子的最大有效电离度为离子强度35％我 = 0.01 M和22％为我 = 0.15M。吸附的有效性与蛋白质以及吸附表面的性质有关。使用带有能量耗散监测的石英晶体微量天平（QCM-D）研究了β-乳球蛋白（LGB）对金表面的功能化。LGB吸附的有效性与金表面的电荷和分子的Zeta电位密切相关。在LGB的正Zeta电位值低于pH 4.8的pH范围内观察到最大吸附质量。该观察结果表明，静电相互作用在金表面上的LGB吸附中起主要作用。基于吸附的质量，确定了金表面上的蛋白质取向。在吸附层中观察到的LGB分子的优先侧向取向与通过蛋白质（MD）的分子动力学模拟确定的分子偶极动量的方向一致。QCM-D方法的使用也使我们能够确定LGB在金表面的吸附效果。知道LGB吸附的机理对于确定将该蛋白固定在固体表面上的最佳条件非常重要。由于β-乳球蛋白是结合各种配体的蛋白质，因此固定化的β-乳球蛋白的结合特性可用于设计生物医学应用中受控的蛋白质结构。QCM-D方法的使用也使我们能够确定LGB在金表面的吸附效果。知道LGB吸附的机理对于确定将该蛋白固定在固体表面上的最佳条件非常重要。由于β-乳球蛋白是结合各种配体的蛋白质，因此固定化的β-乳球蛋白的结合特性可用于设计生物医学应用中受控的蛋白质结构。QCM-D方法的使用也使我们能够确定LGB在金表面的吸附效果。知道LGB吸附的机理对于确定将该蛋白固定在固体表面上的最佳条件非常重要。由于β-乳球蛋白是结合各种配体的蛋白质，因此固定化的β-乳球蛋白的结合特性可用于设计可控的蛋白质结构，以用于生物医学应用。