2025/10/08 by Chiara Bottoni, Matteo Tegoni, Valentina Borghesani · 1 voice
Chemistry · Medicine · Biochemistry, Genetics and Molecular Biology · #Molecular Sensors and Ion Detection #Metal complexes synthesis and properties #Chemical Synthesis and Analysis
paper · doi:10.1021/acs.inorgchem.5c02080
openalex publication_date 2025/10/08 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01
High Resolution Image Download MS PowerPoint Slide In this paper, 4-methylcatechol (4-MC) and L/D-Dopa are selected as target substrates for de novo protein design, serving as a proof-of-concept system for evaluating the catalytic activity of metal coordination sites. We report two novel water-soluble bis-histidyl peptides that exhibit catalytic activity, where structural constraints around the active site would play a pivotal role in metalloenzyme development. The particular tandem His–His motif in the peptides and favorable E 0 ′ enable them to catalyze catechol oxidation reactions efficiently. The coordination behavior of the peptides with Cu(II) and Cu(I) ions is thoroughly investigated using a combination of analytical techniques, including potentiometric titration and fluorescence, ultraviolet–visible (UV–vis), and circular dichroism (CD) spectroscopies. The insights gained into the catalytic binding site and associated pseudocatecholase activity of these peptides contribute to the development of copper-based bioinspired artificial metalloenzymes.