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Capasso Palmiero, U.

Publications and source records attributed to Capasso Palmiero, U..

2 recordsLinked to original sources

Structural heterogeneity in mRNA-LNP subpopulations revealed by AF4-SAXS: implications for cargo loading and cell transfection

Lipid nanoparticles are the leading platform for the delivery of nucleic acid therapeutics, yet their structural complexity remains a significant barrier to achieve rational design and predictable function. Part of this complexity arises from the non-equilibrium assemblies that are difficult to identify using ensemble average techniques given the substantial heterogeneity in all properties. Aiming to overcome the limitations of traditional characterization methods, we combined asymmetric flow field-flow fractionation with in-line small-angle X-ray scattering and spectroscopic analyses, nanoflow cytometry, and cryo-EM to construct detailed structural models of mRNA-loaded nanoparticles formulated with different amounts of mRNA loading (N/P ratios of 3 and 6). This combination of techniques revealed that microfluidic formulation produces structurally diverse nanoparticle subpopulations differing in size, anisotropy, and cargo loading. Notably, these variations extend to the particle internal organization: spheroidal geometries display densely loaded mRNA cores, whereas bleb-like morphologies exhibit reduced mRNA content relative to the lipid amount within segregated domains at the core. NanoFCM further shows that the N/P ratio modulates cargo distribution across individual nanoparticles, with N/P=6 yielding a more uniform mRNA copy number per particle across subpopulations than N/P=3. These differences resulted in higher transfection efficacies for the N/P=6 formulation, highlighting core organization and loading homogeneity as key parameters for efficacious delivery. Together, these results establish a direct link between LNP architecture, internal organization, cargo distribution, and transfection efficiency, underscoring the importance of accounting for heterogeneity in the rational design of nucleic acid delivery systems.

biophysics↗

The interface of condensates of the hnRNPA1 low complexity domain promotes formation of amyloid fibrils

The maturation of liquid-like protein condensates into amyloid fibrils has been associated with neurodegenerative diseases. Here, we analyze the amyloid formation mediated by condensation of the low-complexity domain of hnRNPA1, a protein involved in Amyotrophic Lateral Sclerosis (ALS). We show that phase separation and fibrillation are connected but distinct processes which are independently mediated by different regions of the protein sequence. By monitoring the spatial and temporal evolution of amyloid formation we demonstrate that the formation of fibrils does not occur homogeneously inside the droplets but is promoted at the interface of the condensates. Consistently, we further show that coating the interface of the droplets with surfactant molecules inhibits fibril formation. Our results indicate that the interface of biomolecular condensates can act as an important catalyst for fibril formation, and therefore could represent a possible therapeutic target against the formation of aberrant amyloids mediated by condensation.

biophysics↗