Publications by authors named "Angela Maria Cusano"

Background: Trastuzumab, a therapeutic monoclonal antibody directed against HER2, is routinely used to treat HER2-positive breast cancer with a good response rate. However, concerns have arisen in the clinical practice due to adverse side effects. One way to overcome these limitations is to encapsulate trastuzumab in nanoparticles to improve cytotoxic activity, increase intracellular drug concentrations, escape the immune system and avoid systemic degradation of the drug in vivo.

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Introduction: Currently, conventional treatments of hepatocellular carcinoma (HCC) are not selective enough for tumor tissue and lead to multidrug resistance and drug toxicity. Although sorafenib (SOR) is the standard first-line systemic therapy approved for the clinical treatment of HCC, its poor aqueous solubility and rapid clearance result in low absorption efficiency and severely limit its use for local treatment.

Methods: Herein, we present the synthesis of biodegradable polymeric Poly (D, L-Lactide-co-glycolide) (PLGA) particles loaded with SOR (PS) by emulsion-solvent evaporation process.

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Background: Drug delivery systems based on Human Serum Albumin (HSA) have been widely investigated due to their capability to interact with several molecules together with their nontoxicity, non-immunogenicity and biocompatibility. Sorafenib (SOR) is a kinase inhibitor used as the firstline treatment in hepatic cancer. However, because of its several intrinsic drawbacks (low solubility and bioavailability), there is a growing need for discovering new carriers able to overcome the current limitations.

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Small molecular weight species such as miRNAs and other nucleic acid fragments are gaining an increased interest as biomarkers for relevant diseases. Also, cheap and rapid assays for their routine detection are becoming an urgent need. We have investigated the usability and convenience of a price affordable, label free and fast technique for their detection on a laboratory scale small device based on Bio-Layer Interferometry.

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In this paper, we report on a general approach for the detection of a specific tumoural biomarker directly in serum. Such detection is made possible using a protein-binding peptide selected through an improved phage display technique and then conjugated to engineered microparticles (MPs). Protein biomarkers represent an unlimited source of information for non-invasive diagnostic and prognostic tests; MP-based assays are becoming largely used in manipulation of soluble biomarkers, but their direct use in serum is hampered by the complex biomolecular environment.

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Extremities of proteins are potent sites for functionalization. Carboxy terminus variants of the Trametes sp. strain C30 LAC3 laccase were generated and produced in Saccharomyces cerevisiae.

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The aim of the present work is the study of the bacteriostatic/bactericidal effect of a silver-containing mesoporous bioactive glass obtained by evaporation-induced self-assembly and successive thermal stabilization. Samples of the manufactured mesophase were characterized by means of transmission electron microscopy and N₂ adsorption/desorption at 77 K, revealing structural and textural properties similar to SBA-15 mesoporous silica. Glass samples used for bioactivity experiments were put in contact with a standardized, commercially available cell culture medium instead of lab-produced simulated body fluid, and were then characterized by means of X-ray diffraction, field emission scanning electron microscopy and Fourier transform infrared spectroscopy.

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The formation of a dense monolayer of histidine-tagged recombinant laccase on gold electrodes by using a short thiol-NTA linker is described, as well as a kinetic analysis of the process by cyclic voltammetry. From a detailed analysis of the catalytic reduction of dioxygen by laccase in the presence of a one-electron redox mediator it can be concluded that the immobilized enzyme remains as active as in homogeneous solution.

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Background: The final aim of recombinant protein production is both to have a high specific production rate and a high product quality. It was already shown that using cold-adapted bacteria as host vectors, some "intractable" proteins can be efficiently produced at temperature as low as 4 degrees C.

Results: A novel genetic system for the production and secretion of recombinant proteins in the Antarctic Gram-negative bacterium Pseudoalteromonas haloplanktis TAC125 was set up.

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The nature and location of structural features responsible for the secretion of a cold-adapted alpha-amylase in the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125 was studied by deletion mutagenesis of the wild-type enzyme and of chimerical proteins derived from the fusion of the alpha-amylase with a reporter enzyme. Domain C of the psychrophilic alpha-amylase contains secretion features involved in extracellular targeting.

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