"CLICK CHEMISTRY" ASSEMBLY OF HIV PROTEASE INHIBITORS

HIV蛋白酶抑制剂的“点击化学”组装

• 批准号: 8169341
• 负责人: KARL BARRY SHARPLESS
• 金额: $ 1.13万
• 依托单位: UNIVERSITY OF CALIFORNIA, SAN DIEGO
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-05-01 至 2011-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8169341
• 关键词: Chemistry; Computer Retrieval of Information on Scientific Projects Database; Docking; Drug resistance; Evolution; Face; Funding; Grant; HIV Protease; HIV Protease Inhibitors; In Situ; Institution; Nature; Peptide Hydrolases; Protease Inhibitor; Research; Research Personnel; Resistance; Resources; Source; Therapeutic; United States National Institutes of Health; flexibility; 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.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 HIV蛋白酶靶标的性质和重要性是众所周知的。 抗药性进化的问题是 现在被认为是有效的长期治疗的主要障碍。 新的合成方法，指导 通过计算对接，有望产生更有效的HIV蛋白酶抑制剂， 抗战在蛋白酶突变体背景下利用“点击化学”原位合成抑制剂的可能性 指出了一个新的灵活的方法来解决这个问题。