Ferdinando Mercuri

Structural studies of the C-terminal cysteine-rich domain of Aedes albopictus vitellogenin reveal an evolutionarily divergent, monomeric C-terminal cysteine knot (CTCK) architecture

This study determines the crystal structure of the C-terminal cysteine knot domain of Aedes albopictus vitellogenin, revealing a monomeric, evolutionarily divergent architecture that challenges prior assumptions about its oligomerization role.

Enantiopurity-Dependent Peptide Coacervates and Asymmetric Organocatalysis

This study shows that enantiopure peptide coacervates form stable liquid droplets and exhibit enantioselective catalytic activity, while racemic mixtures form solid precipitates.