Impact of the Histidine-Triazole and Tryptophan-Pyrene Exchange in the WHW Peptide: Cu(II) Binding, DNA/RNA Interactions and Bioactivity.

ABSTRACT: In three novel peptidoids based on the tryptophan-histidine-tryptophan (WHW) peptide, the central histidine was replaced by Ala-(triazole), and two derivatives also had one tryptophan replaced with pyrene-alkyls of different lengths and flexibility. Pyrene analogues show strong fluorescence at 480-500 nm, attributed to intramolecular exciplex formation with tryptophan. All three peptidoids bind Cu²⁺ cation in water with strong affinity, with Trp- Ala-(triazole)-Trp binding comparably to the parent WHW, and the pyrene analogues even stronger, demonstrating that replacement of histidine with triazole in peptides does not hamper Cu²⁺ coordination. The studied peptidoids strongly bind to ds-DNA and ds-RNA, whereby their complexes with Cu²⁺ exhibit distinctively

SUBMITTER: Krosl I 

PROVIDER: S-EPMC9266797 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature