Intact and consistent protein biosynthesis relies on the ability of the ribosome to stay in the correct open reading frame (ORF) during translation.

[2] However, a shift in the ORF is not universally deleterious, as many viruses capitalize on this phenomenon by using a programmed ribosomal frameshift (PRF) to translate several proteins from the same sequence, thereby maximizing the storage capacity of their genome.

As a result, the HIV-1 ribosomal frameshift signal is highly regulated, as it modulates the expression levels of the Gag protein relative to the Gag-Pol polyprotein.

[4][5] The HIV-1 ribosomal frameshift signal requires two cis-acting elements: a heptameric "slippery site" and a downstream secondary RNA structure separated by an 8-nucleotide spacer.

[3][4] This heptamer is inherently "slippery", as data has shown that even in the absence of the downstream secondary RNA structure, frameshifting still occurs at roughly 0.0001% to 0.1% per codon.

The lead compound is symmetrical whereas the target downstream secondary RNA structure is non-symmetrical, suggesting that both supposed intercalators are necessary for high-affinity binding.