ArticleInorganic chemistry2026
Dual Amino Acid Swap in MUC7-Derived Peptide Enhances Resistance and Modulates Zn(II) and Cu(II) Complex Stability, Secondary Structure and Antimicrobial Activity.
Article in Inorganic chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed.
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Authors and funding
6 authors.
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Abstract
Metal ion complexes with antimicrobial peptides are emerging as promising therapeutic agents, but their efficacy is often limited by rapid proteolytic degradation and poorly understood metal-driven mechanisms. Here, we stabilize a sequence derived from mucin 7 by introducing two d-amino acids at the site most susceptible to proteolytic cleavage and show that this subtle modification rewires its copper(II) and zinc(II) coordination chemistry and antimicrobial activity. The coordination, structure and activity of the modified peptide (peptidomimetic) with Cu(II) and Zn(II) were probed by potentiometry, mass spectrometry, multiple spectroscopies and quantum-chemical calculations, together with antimicrobial and antibiofilm assays. The peptidomimetic is resistant to enzymatic cleavage and forms thermodynamically more stable Cu(II) complexes with {3N
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