唾液酸糖表位类人源化N-糖基化修饰治疗性重组蛋白的研究进展

Advances on the human-like N-glycosylation of sialylated glycoepitopes in therapeutic recombinant proteins

摘要:

唾液酸化N-糖基化修饰重组蛋白能提高治疗性蛋白的理化性质，如延长半衰期、增强组织穿透性以及抑制炎症反应等。但迄今为止糖蛋白的N-糖基化修饰效率和唾液酸化效率都很难达到100%，这导致了唾液酸修饰糖基化重组蛋白的均质化、规模化生产非常困难。因而提高类人源化N-糖基化修饰治疗性重组蛋白的均质性仍是目前糖蛋白药物研发任务之一。该文围绕提高唾液酸糖表位N-糖基化修饰治疗性重组蛋白效率的方法及均质化类人源化唾液酸糖表位治疗性重组蛋白的生产途径展开综述。

Abstract:

Sialylation can improve the physicochemical properties of therapeutic recombinant proteins, such as prolonging the half-life, enhancing the penetrating power and inhibiting inflammatory responses. However, the efficiency of N-glycosylation and sialylation hardly reaches 100%, bringing about the difficulty in homogeneous and large-scale production of sialylated recombinant proteins. Therefore, strengthening the homogeneity of human-like N-glycosylated therapeutic recombinant proteins still represents one of the foci of glycoprotein drug development. This review is centered on the approaches to increasing the efficiency of N-glycosylation of therapeutic recombinant proteins and the production process of homogeneous human-like N-glycosylation of sialylated glycoepitopes in therapeutic recombinant proteins.