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.

Department of Biophysics Faculty of Science Palacky University in Olomouc Slechtitelu 27 CZ 78371 Olomouc Czech Republic

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

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