ArticleInorganic chemistry2023
Zn(II) Induces Fibril Formation and Antifungal Activity in Shepherin I, An Antimicrobial Peptide from
Article in Inorganic chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Beyond proteolysis: rational modification of mucin-derived peptidomimetics with enhanced metal-mediated antimicrobial activity.RSC advances · 2026Article
- Modulating Copper(II) Coordination and Antimicrobial Activity: Effects of d-Amino Acid Substitution andInorganic chemistry · 2025Article
- Systematic Model Peptide Studies: A Crucial Step To Understand the Coordination Chemistry of Mn(II) and Fe(II) in Proteins.Inorganic chemistry · 2025Article
- Cu(ii) binding to an antimicrobial shrimp peptide - a small step for structural chemistry, a big leap for medicinal applications.Chemical science · 2025Article
- Bioinorganic Chemistry Meets Microbiology: Copper(II) and Zinc(II) Complexes Doing the Cha-Cha with the C-t-CCL-28 Peptide, Dancing till the End of Microbes.Inorganic chemistry · 2024Article
- Phytochemicals, Two New Sulphur Glycosides and Two New Natural Products, from Shepherd's Purse Seed and Their Activities.Molecules (Basel, Switzerland) · 2024Article
- Insights into the Chemistry, Structure, and Biological Activity of Human Salivary MUC7 Fragments and Their Cu(II) and Zn(II) Complexes.Inorganic chemistry · 2024Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Shepherin I is a glycine- and histidine-rich antimicrobial peptide from the root of a shepherd's purse, whose antimicrobial activity was suggested to be enhanced by the presence of Zn(II) ions. We describe Zn(II) and Cu(II) complexes of this peptide, aiming to understand the correlation between their metal binding mode, structure, morphology, and biological activity. We observe a logical sequence of phenomena, each of which is the result of the previous one: (i) Zn(II) coordinates to shepherin I, (ii) causes a structural change, which, in turn, (iii) results in fibril formation. Eventually, this chain of structural changes has a (iv) biological consequence: The shepherin I-Zn(II) fibrils are highly antifungal. What is of particular interest, both fibril formation and strong anticandidal activity are only observed for the shepherin I-Zn(II) complex, linking its structural rearrangement that occurs after metal binding with its morphology and biological activity.
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