Interactions of carrageenan or its degradation product with R15K by affinity capillary electrophoresis  

亲和毛细管电泳法研究卡拉胶及其降解产物与R15K的相互作用（英文）

作　　者：李中杰[1,2] 李立[1,2] 王孝伟[1,2] 刘俊义[1,2] 凌笑梅[1,2] 

机构地区：[1]北京大学药学院天然药物及仿生药物国家重点实验室 [2]化学生物学系,北京100191

出　　处：《Journal of Chinese Pharmaceutical Sciences》2015年第6期400-404,共5页中国药学（英文版）

基　　金：National Natural Science Foundation(Grant No.81373372);Specialized Research Fund for the Doctoral Program of Higher Education of China(Grant No.20110001110021 and 20130001110059)

摘　　要：V3 loop of HIV-1 envelop protein gp120 plays a pivotal role in the entry process of HIV-1 into target cells. R15K, the relatively conserved region of V3 loop, can be used in binding studies instead of recombinant gp120 molecule. Polyanionic compounds, such as carrageenan, possess antiviral activity through disrupting gp120-CD4 interaction, and chemical modifications have been performed to improve such activity. In this work, we, for the first time, analyzed the interactions between carrageenan or its degradation and R15K by affinity capillary electrophoresis （ACE）. Our results revealed that depolymerized carrageenan rather than carrageenan could bind to R15K. The binding constant of depolymerized carrageenan was （2.94±0.57）× 10^6 mol/L. Our finding indicated that the depolymerized carrageenan could be R15K antagonist, and it might inhibit the infection of HIV-1 through the entry process.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。

关 键 词：HIV-1 V3 peptides ACE CARRAGEENAN Carrageenan degradation 

分 类 号：O658.9[理学—分析化学] R285[理学—化学]