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Giorgia Brancolini

Publications and source records attributed to Giorgia Brancolini.

2 recordsLinked to original sources

Graphene Electric Double-Layer Transistors for Enhanced-Sensitivity Label-Free Detection of Human Serum Albumin

Accurate detection of human serum albumin (HSA) is essential for the early diagnosis and monitoring of renal and hepatic disorders. We present a graphene-based electrolyte-gated field-effect transistor (EGFET) for label-free, real-time quantification of HSA under non-Faradaic operation. Devices exploit the high interfacial capacitance of the electric double layer (EDL) to transduce electrostatic perturbations induced by albumin adsorption into measurable conductance modulation. Negatively charged HSA molecules induce systematic modulation of the graphene channel, producing a concentration-dependent displacement of the Dirac voltage consistent with p-type doping. To establish a molecular-level interpretation of the sensing response, Brownian Dynamics simulations show that HSA adsorbs onto graphene through multiple adsorption orientations associated with heterogeneous interfacial charge distributions and variable dipole alignments relative to the surface. Adsorption is energetically stabilized by van der Waals interactions. Analysis of transfer characteristics across concentrations ranging from 0.01 to 30mgmL-1 reveals a correlation between surface charge density and carrier transport modulation within the electric double layer. Optimized devices exhibit a limit of detection of 0.0087 mg mL-1 and a linear dynamic range extending to 10 mg mL-1. The response remains non-Faradaic under sub-volt operation with reversible and reproducible behavior. The use of an inverse-mobility analytical metric highlights the role of disorder-enhanced carrier scattering in signal amplification, enabling sensitive electrostatic detection while preserving reversible device operation. These results establish liquid-gated graphene EGFETs as a promising platform for quantitative protein sensing and provide insight into disorder-mediated transport mechanisms in graphene bioelectronic devices.

cond-mat.mes-hall↗

Citrate stabilized gold nanoparticles interfere with amyloid fibril formation: D76N and ΔN6 \b{eta}2-microglobulin variants

Protein aggregation including the formation of dimers and multimers in solution, underlies an array of human diseases such as systemic amyloidosis which is a fatal disease caused by misfolding of native globular proteins damaging the structure and function of affected organs. Different kind of interactors can interfere with the formation of protein dimers and multimers in solution. A very special class of interactors are nanoparticles thanks to the extremely efficient extension of their interaction surface. In particular citrate-coated gold nanoparticles (cit-AuNPs) were recently investigated with amyloidogenic protein $β$2-microglobulin ($β$2m). Here we present the computational studies on two challenging models known for their enhanced amyloidogenic propensity, namely $Δ$N6 and D76N $β$2m naturally occurring variants, and disclose the role of cit-AuNPs on their fibrillogenesis. The proposed interaction mechanism lies in the interference of the cit-AuNPs with the protein dimers at the early stages of aggregation, that induces dimer disassembling. As a consequence, natural fibril formation can be inhibited. Relying on the comparison between atomistic simulations at multiple levels (enhanced sampling molecular dynamics and Brownian dynamics) and protein structural characterisation by NMR, we demonstrate that the cit-AuNPs interactors are able to inhibit protein dimer assembling. As a consequence, the natural fibril formation is also inhibited, as found in experiment.

q-bio.BM↗