A biological membrane is a structure characteristic for various cells and organelles present in almost all living organisms. Even though, it is one of the most common structures in organisms, where it serves crucial functions, a phospholipid bilayer may also take part in pathological processes leading to severe diseases. Research indicates that biological membranes have a profound impact on the pathological processes of oligomerization of amyloid-forming proteins. These processes are a hallmark of amyloid diseases, a group of pathological states involving, e.g., Parkinson's or Alzheimer's disease. Even though amyloidogenic diseases reap the harvest in modern societies, especially in elderly patients, the mechanisms governing the amyloid deposition are not clearly described. Therefore, the presented study focuses on the description of interactions between a model biological membrane (POPG) and one of amyloid forming proteins – human cystatin C. For the purpose of the study molecular dynamics simulations were applied to confirm interactions between the protein and POPG membrane. Next the NMR techniques were used to verify how the data obtained in solution compared to MD simulations and determine fragments of the protein responsible for interactions with POPG. Finally, circular dichroism was used to monitor the changes in secondary structure of the protein and size exclusion chromatography was used to monitor its oligomerization process. Obtained data indicates that the protein interacts with POPG submerging itself into the bilayer with the AS region. However, the presence of POPG bilayer does not significantly affect the structure or oligomerization process of human cystatin C.

生物膜是几乎所有生物体中存在的各种细胞和细胞器的结构特征。尽管它是生物体中最常见的结构之一，发挥着至关重要的功能，但磷脂双层也可能参与导致严重疾病的病理过程。研究表明，生物膜对淀粉样蛋白寡聚的病理过程具有深远的影响。这些过程是淀粉样蛋白疾病的标志，淀粉样蛋白疾病是一组涉及帕金森病或阿尔茨海默病的病理状态。尽管淀粉样蛋白生成性疾病在现代社会，尤其是老年患者中屡见不鲜，但控制淀粉样蛋白沉积的机制尚不清楚。因此，本研究重点描述模型生物膜 (POPG) 和一种淀粉样蛋白形成蛋白 - 人半胱氨酸蛋白酶抑制剂 C 之间的相互作用。为了研究的目的，应用分子动力学模拟来确认蛋白质和 POPG 膜之间的相互作用。接下来，使用 NMR 技术验证溶液中获得的数据与 MD 模拟相比如何，并确定负责与 POPG 相互作用的蛋白质片段。最后，利用圆二色性监测蛋白质二级结构的变化，利用尺寸排阻色谱监测其寡聚过程。获得的数据表明该蛋白质与 POPG 相互作用，将其自身浸入具有 AS 区域的双层中。然而，POPG双层的存在并不显着影响人胱抑素C的结构或​​寡聚过程。