铁(II)超分子螺旋体干扰 HIV-1 Tat-TAR RNA 相互作用，这对病毒复制至关重要。

Institute of Biophysics, Academy of Sciences of the Czech Republic, v.v.i., Kralovopolska 135, CZ-61265 Brno, Czech Republic.

School of Chemistry, University of Birmingham, Edgbaston, Birmingham B152TT, United Kingdom.

Sci Rep. 2016 Jul 12;6:29674. doi: 10.1038/srep29674.

The interaction between the HIV-1 transactivator protein Tat and TAR (transactivation responsive region) RNA, plays a critical role in HIV-1 transcription. Iron(II) supramolecular helicates were evaluated for their in vitro activity to inhibit Tat-TAR RNA interaction using UV melting studies, electrophoretic mobility shift assay, and RNase A footprinting. The results demonstrate that iron(II) supramolecular helicates inhibit Tat-TAR interaction at nanomolar concentrations by binding to TAR RNA. These studies provide a new insight into the biological potential of metallosupramolecular helicates.

HIV-1 转录激活蛋白 Tat 与 TAR（转录激活反应区）RNA 之间的相互作用在 HIV-1 转录中起着关键作用。采用紫外熔融实验、电泳迁移率变动分析和 RNase A 足迹实验，评估了铁（II）超分子螺旋体抑制 Tat-TAR RNA 相互作用的体外活性。结果表明，铁（II）超分子螺旋体通过与 TAR RNA 结合，在纳摩尔浓度下抑制 Tat-TAR 相互作用。这些研究为金属超分子螺旋体的生物学潜力提供了新的见解。