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.

Keywords: HIF‐1α; electrophoretic gel mobility shift assay; i‐motif; structural dynamics; tryptophan‐rich peptide.