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微生物体内的70 ku热休克蛋白407-426片段可以有效刺激体内CD40+抗原递呈细胞如DC,单核细胞等的成熟,可有效刺激体内产生IL12和TNFα,被认为是CD40L的替代配体,因此对免疫系统有着重要的意义。同时,该片段还可以有效结合外源蛋白分子,因此又是天然的递呈抗原的载体佐剂。该文章以开发新型载体佐剂为目的,使用Discovery studio软件分析经过单片段与两次串联的该肽段结构并预测了它们与CD40分子进行对接后的复合物。经过分析其关键结合位点,阐明了该肽段与CD40分子间参与相互作用的残基,并发现经过2次串联的肽段确实可以比单片段更有效的与CD40进行相互作用。因此,实验结果可为新型肿瘤疫苗的设计提供理论依据。
Microbial 70 ku HSP 407-426 fragment can effectively stimulate the maturation of CD40 + antigen-presenting cells such as DCs and monocytes, effectively stimulating the production of IL12 and TNFα in vivo and is considered as a substitute ligand for CD40L. The immune system has important significance. At the same time, the fragment can also effectively bind foreign protein molecules, and therefore is a natural antigen presenting carrier adjuvant. In this paper, with the aim of developing a new vector adjuvant, we used Discovery Studio software to analyze the structure of the peptides after single-stranded and double-stranded in series, and predicted their complexes with CD40 molecules. After analyzing its key binding sites, we elucidated the residues involved in the interaction between this peptide and CD40 molecules, and found that peptides that pass through two in series can indeed interact with CD40 more efficiently than single fragments. Therefore, the experimental results can provide a theoretical basis for the design of novel tumor vaccines.