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Designer tryptophan-rich peptide modulates structural dynamics of HIF-1α DNA i-motif DNA. | LitMetric

AI Article Synopsis

  • - Cytosine-rich DNA sequences can form unique structures called i-motifs through special hydrogen bonding, impacting their stability and function.
  • - Molecular probes are important for understanding how these i-motifs behave and their roles in cells.
  • - A decapeptide called WK, made of alternating tryptophan and lysine, shows promise in influencing the structure of the HIF-1α DNA i-motif, aiding in the design of new study tools for i-motifs.

Article 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. WK, 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.

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Source
http://dx.doi.org/10.1002/psc.3601DOI Listing

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