期刊
JOURNAL OF MEDICINAL CHEMISTRY
卷 61, 期 19, 页码 8734-8745出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jmedchem.8b00890
关键词
-
资金
- National Science Foundation of China [81573266, 81630090]
- Beijing Nova Program [Z181100006218115]
- National Science and Technology Major Project of China [2018ZX09711003]
- National Key Research and Development Program of China [2016YFC1201000, 2016YFC1200400]
Class I enveloped viruses share similarities in their apparent use of a hexameric coiled-coil assembly to drive the merging of virus and host cell membranes. Inhibition of coiled coil-mediated interactions using bioactive peptides that replicate an alpha-helical chain from the viral fusion machinery has significant antiviral potential. Here, we present the construction of a series of lipopeptides composed of a de novo heptad repeat sequence-based alpha-helical peptide plus a hydrocarbon tail. Promisingly, the constructs adopted stable alpha-helical conformations and exhibited relatively broad-spectrum antiviral activities against Middle East respiratory syndrome coronavirus (MERS-CoV) and influenza A viruses (IAVs). Together, these findings reveal a new strategy for relatively broad-spectrum antiviral drug discovery by relying on the tunability of the alpha-helical coiled-coil domains present in all class I fusion proteins and the amphiphilic nature of the individual helices from this multihelix motif.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据