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HIV-1包膜蛋白gp120的V3 loop区在HIV-1病毒进入靶细胞的过程中发挥着关键的作用。V3 loop区中相对保守的区域R15K,可代替重组gp120分子用于结合实验的研究。聚阴离子化合物如卡拉胶,可通过干扰gp120与CD4的相互作用发挥抗病毒的活性,并且已有研究通过对其进行结构修饰来提高其抗病毒的活性。本实验首次采用亲和毛细管电泳的方法研究卡拉胶及其降解产物与R15K的相互作用,并且我们得到的结论为卡拉胶降解产物可与R15K结合,结合常数为(2.94±0.57)×106 mol/L。该结果提示卡拉胶降解可能为R15K拮抗剂,可通过拮抗HIV-1病毒的进入过程来抑制HIV-1的感染。
The V3 loop region of HIV-1 envelope protein gp120 plays a key role in HIV-1 viral entry into target cells. The relatively conserved region R15K in the V3 loop region can be used in place of the recombinant gp120 molecule for binding studies. Polyanionic compounds such as carrageenan exert anti-viral activity by interfering with the interaction of gp120 with CD4 and it has been studied to enhance its antiviral activity by structurally modifying it. In this study, the interaction between carrageenan and its degradation products and R15K was studied for the first time by affinity capillary electrophoresis, and we concluded that the degradation products of carrageenan could bind to R15K with a binding constant of (2.94 ± 0.57) × 106 mol / L. This result suggests that the degradation of carrageenan may be an antagonist of R15K, which can inhibit HIV-1 infection by antagonizing the entry of HIV-1 virus.