• 我要登录|
  • 免费注册
    |
  • 我的丁香通
    • 企业机构:
    • 成为企业机构
    • 个人用户:
    • 个人中心
  • 移动端
    移动端
丁香通 logo丁香实验_LOGO
搜实验

    大家都在搜

      大家都在搜

        0 人通过求购买到了急需的产品
        免费发布求购
        发布求购
        点赞
        收藏
        wx-share
        分享

        Identifying and Characterizing HIV Protease Inhibitors

        互联网

        728
        HIV protease catalyzes the hydrolysis of specific peptide bonds of viral polyproteins, thus processing these polyproteins into their active components. These protein processing reactions are requisite for viral replication. Therefore, the HIV protease is an ideal target for the chemotherapeutic treatment of HIV disease (1 3 ). HIV protease is an aspartyl protease,and the aspartyl protease inhibitor, pepstatin, was one of the first identified inhibitors of HIV protease. More potent inhibitors have been designed and synthesized since, in fact, four protease inhibitors—saquinavir (Ro-31,8959), ritonavir (ABT-538), indinavir (L-735,524), and Nelfinavir (AG1343)—are effective in clinical trials to treat HIV disease (4 6 ) and recently were approved by the Food and Drug Administration for the chemotherapeutic treatment of HIV infections. Other protease inhibitors in clinical trials are VX-478 (141W94) and ABT-378. Notwithstanding these early successes, it is difficult to comply with these drug’s dosing regiments. Furthermore, viral resistance to individual inhibitors and cross-resistance to multiple inhibitors occur in vivo (7 ,8 ). Therefore, a medical need still exists for new HIV protease inhibitors with different resistance profiles.
        ad image
        提问
        扫一扫
        丁香实验小程序二维码
        实验小助手
        丁香实验公众号二维码
        扫码领资料
        反馈
        TOP
        打开小程序