Giulio Alberini

The paper designs a high-affinity CLDN5 peptide binder, ST9, that induces reversible, size-controlled BBB openings without altering CLDN5 expression or proteomic profile.

This study investigates how gain-of-function variants in the Kv7.2 channel's activation gate stabilize a partially open conformation, enabling K+ permeation and linking it to neurodevelopmental disorders.

The paper models the blood-brain barrier tight junctions using multi-pore structures and shows that multi-Pore I replicates the permeability effect of a Cldn5 mutation.

The paper designs and tests peptides that bind claudin-5 to increase blood-brain barrier permeability, identifying a peptide that effectively enhances permeability in vitro.

This study identifies two KCNQ2 variants causing developmental encephalopathies by constitutively opening the Kv7.2 pore activation gate, leading to gain-of-function effects.

This study uses Molecular Dynamics simulations to compare ion and water permeability of Cldn10b and Cldn15 paracellular channels, revealing structural determinants of their permeability properties.

The paper uses molecular dynamics simulations to study how pathogenic and artificial mutations affect ion selectivity in Claudin-5 paracellular pores, identifying structural models that align with experimental observations.

This study compares two structural models of Claudin-5 complexes in BBB tight junctions using molecular dynamics and free energy calculations to assess their ionic transport properties.