Abstract：
Herein, we aimed to highlight current \"gaps\" in the understanding of the potential interactions between the Anle138b isomer ligand, a promising agent for clinical research, and the intrinsically disordered alpha-synuclein protein. The presence of extensive unstructured areas in alpha-synuclein determines its existence in the cell of partner proteins, including the cyclophilin A chaperone, which prevents the aggregation of alpha-synuclein molecules that are destructive to cell life. Using flexible and cascaded molecular docking techniques, we aimed to expand our understanding of the molecular architecture of the protein complex between alpha-synuclein, cyclophilin A and the Anle138b isomer ligand. We demonstrated the possibility of intricate complex formation under cellular conditions and revealed that the main interactions that stabilize the complex are hydrophobic and involve hydrogen.
摘要：
在这里，我们的目的是强调目前的“差距”在理解之间的潜在相互作用的Anle138b异构体配体，一个有前途的临床研究的代理人，和内在无序的α-突触核蛋白。α-突触核蛋白中广泛的非结构化区域的存在决定了其在伴侣蛋白细胞中的存在，包括亲环蛋白A伴侣,这可以防止破坏细胞生命的α-突触核蛋白分子的聚集。使用灵活的级联分子对接技术，我们的目的是扩大我们对α-突触核蛋白之间的蛋白质复合物的分子结构的理解，亲环蛋白A和Anle138b异构体配体。我们证明了在细胞条件下复杂复合物形成的可能性，并揭示了稳定复合物的主要相互作用是疏水的并涉及氢。
