CERM/CIRMMP Infrastructure

@cerm-cirmmp.bsky.social

CERM/CIRMMP is a NMR infrastructure for Life Sciences, which provides a unique environment for research in the field of Structural Biology. https://www.cerm.unifi.it/

The programme will include a keynote lecture, interactive roundtables, and a session on the current state of the art and research gaps, with a focus on identifying priorities for future action.

Are you interested in these topics? The @fheritale.bsky.social consortium invites stakeholders from across the research landscape to join us: 📍 Brussels 🗓️ 26 May. Researchers, industry, and policymakers are welcome to contribute! For more information: fheritale.eu/stakeholder-...

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FHERITALE@fheritale.bsky.social · 4mo ago

On #WorldHealthDay, we want to highlight the potential impact of micro and nanoplastics on human health via inflammation, oxidative stress, and the delivery of toxic chemicals or pathogens. For a comprehensive overview, see our Strategic technology and service needs: zenodo.org/records/1938...

New insights into α-synuclein interactions via NMR & MD, supported by @instruct-eric.bsky.social and #ITACA.SB! Read the full article here 👇

Molecular Interplay of Small Molecules and Calcium Ions with α-Synuclein Revealed by NMR and Molecular Dynamics Simulations

Human α-synuclein is an intrinsically disordered protein concentrated at presynaptic terminals and strongly linked to Parkinson’s disease and other synucleinopathies. Its dynamic C-terminal region mediates interactions with small molecules and metal ions. Here, we used high-resolution nuclear magnetic resonance spectroscopy (NMR) and molecular dynamics (MD) simulations to characterize interactions between the C-terminal α-synuclein construct, the small molecule fasudil, and calcium ions. NMR data show that fasudil and Ca2+ bind preferentially to overlapping regions enriched in alternating tyrosine and acidic residues while preserving the protein’s disordered nature. Side-chain-resolved spectra indicate distinct driving forces for fasudil and calcium binding. MD simulations reveal that Ca2+ modifies the local electrostatic environment, decreasing fasudil interaction frequency through electrostatic screening and steric effects. Despite this, fasudil retains dynamic, reversible contacts with key tyrosine residues. Overall, exposed α-synuclein conformations allow simultaneous, ligand-specific interactions, highlighting side-chain hotspots governing binding in Ca2+-rich conditions.

pubs.acs.org