Designer tryptophan‐rich peptide modulates structural dynamics of HIF‐1α DNA i‐motif DNA

Abstract

Cytosine‐rich DNA sequences can fold into intercalated motifs known as i‐motifs, through noncanonical hydrogen bonding interactions. Molecular probes can provide valuable insights into the conformational stability and potential cellular functions of i‐motifs. W5K5, a decapeptide composed of alternating tryptophan (W) and lysine (K) units, has been identified as a lead candidate to modulate the structural dynamics of the hypoxia‐inducible factor 1‐alpha (HIF‐1α) DNA i‐motif. This finding is expected to facilitate the rational design of peptide‐based probes for studying the structure and functional dynamics of i‐motifs.