"CLICK CHEMISTRY" ASSEMBLY OF HIV PROTEASE INHIBITORS

HIV蛋白酶抑制剂的“点击化学”组装

• 批准号: 7601656
• 负责人: KARL BARRY SHARPLESS
• 金额: $ 3.82万
• 依托单位: UNIVERSITY OF CALIFORNIA, SAN DIEGO
• 依托单位国家: 美国
• 财政年份: 2007
• 资助国家: 美国
• 起止时间: 2007-05-01 至 2008-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7601656
• 关键词: Chemistry; Computer Retrieval of Information on Scientific Projects Database; Docking; Drug resistance; Endopeptidases; Evolution; Face; Funding; Grant; HIV Protease; HIV Protease Inhibitors; In Situ; Institution; Nature; Peptide Hydrolases; Personal Satisfaction; Protease Inhibitor; Research; Research Personnel; Resistance; Resources; Source; Therapeutic; United States National Institutes of Health; inhibitor/antagonist; mutant; novel

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The nature and importance of the HIV protease target is well known. The problem of the evolution of drug resistance is now recognized as a major impediment to effective long-term therapeutic treatment. Novel synthetic approaches, guided by computational docking hold the promise of generating more effective HIV protease inhibitors, that are robust in the face of resistance. The possibilities of in situ synthesis of inhibitors utilizing "click chemistry" in the context of protease mutants points to a new flexible approach to this problem.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目及 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 HIV蛋白酶靶标的性质和重要性是众所周知的。 耐药性演变问题现在被认为是有效长期治疗的主要障碍。 在计算对接的指导下，新颖的合成方法有望产生更有效的 HIV 蛋白酶抑制剂，这些抑制剂在面对耐药性时具有强大的稳定性。在蛋白酶突变体的背景下利用“点击化学”原位合成抑制剂的可能性指出了解决该问题的新的灵活方法。