Zn(II) Induces Fibril Formation and Antifungal Activity in Shepherin I, An Antimicrobial Peptide from Capsella bursa-pastoris

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.

Automated summary

The correlation between metal binding mode, structure, morphology, and biological activity of shepherin I-Zn-(II) and shepherin I-Cu-(II) complexes are investigated. It is found that the binding of Zn-(II) ions to shepherin I leads to structural changes and fibril formation, resulting in strong antifungal activity. In contrast, the shepherin I-Cu-(II) complex does not exhibit the same effects.