Sabín Juan, Prieto Gerardo, Ruso Juan M, Messina Paula V, Salgado Francisco J, Nogueira Montserrat, Costas Miguel, Sarmiento Félix
Grupo de Biofísica e Interfases, Departamento de Física Aplicada, Facultad de Física, Universidad de Santiago de Compostela, Santiago de Compostela, Spain.
J Phys Chem B. 2009 Feb 12;113(6):1655-61. doi: 10.1021/jp804641e.
The interaction between two serum blood proteins, namely human serum albumin (HSA) and human immunoglobulin G (IgG), with 1,2-dimyristoyl-sn-glycero-3-phosphatidylcholine (DMPC) liposomes has been studied in detail using dynamic light scattering, flow cytometry, enzyme-linked immunosorbent assay (ELISA), electrophoretic mobility, differential scanning calorimetry (DSC), and surface tension measurements. HSA and IgG interact with liposomes forming molecular aggregates that remain stable at protein concentrations beyond those of total liposome coverage. Both HSA and IgG penetrate into the liposome bilayer. An ELISA assay indicates that the Fc region of IgG is the one that is immersed in the DMPC membrane. The liposome-protein interaction is mainly of electrostatic nature, but an important hydrophobic contribution is also present.
利用动态光散射、流式细胞术、酶联免疫吸附测定（ELISA）、电泳迁移率、差示扫描量热法（DSC）和表面张力测量等方法，对两种血清蛋白，即人血清白蛋白（HSA）和人免疫球蛋白G（IgG）与1,2-二肉豆蔻酰-sn-甘油-3-磷脂酰胆碱（DMPC）脂质体之间的相互作用进行了详细研究。HSA和IgG与脂质体相互作用形成分子聚集体，在蛋白质浓度超过总脂质体覆盖浓度时仍保持稳定。HSA和IgG都能穿透脂质体双层。ELISA分析表明，IgG的Fc区域是浸入DMPC膜中的区域。脂质体与蛋白质的相互作用主要是静电性质，但也存在重要的疏水作用。
