Publications by authors named "Raffaella Lettieri"

Vascular Endothelial Growth Factor C (VEGFC) is a promising biological drug, with preclinical studies indicating its potential for treating myocardial infarction, neurodegenerative diseases, and lymphedema, a condition that currently lacks curative treatment. While adenoviral VEGFC gene therapy has progressed to phase II studies, its clinical efficacy is limited by rapid immune inactivation. This study explores lignin nanoparticles (LNPs) as an alternative VEGFC delivery system.

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Plastics are widely produced due to their stability and ease of manufacturing, but many of them quickly become a waste, breaking down into microplastics and nanoplastics. While methods for the identification and characterization of plastic particles are well consolidated, the small size of nanoplastics presents challenges for their detection and analysis. Furthermore, due to the difficulty of identifying nanoplastics, analytical studies concerning their effect on cells and a comprehensive spectroscopic characterization are still lacking.

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Article Synopsis
  • The study explores how adding natural additives to a new compostable bioplastic made from milk scraps can improve its mechanical strength and thermal stability for practical use.
  • Incorporating 2 mm and 10 mm long fibers increased the ductility and compressive strain significantly, enhancing the material's overall performance without compromising compostability.
  • The combination of fibers and organic particulates resulted in a stronger, more durable bioplastic, demonstrating excellent compatibility and improved thermal stability, highlighting the ecological benefits of using natural reinforcement agents.
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Structures composed of alternating α and β amino acids can give rise to peculiar secondary structural motifs, which could self-assemble into complex structures of controlled geometries. This work describes the self-assembly properties of an α,β-peptide, containing three units of H2-(2-F-Phe)-h-PheGly-OH, able to self-organize on surfaces into a fascinating supramolecular rope. This material was characterized by AFM, electronic conduction and fluorescence measurements.

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External stimuli are potent tools that Nature uses to control protein function and activity. For instance, during viral entry and exit, pH variations are known to trigger large protein conformational changes. In Nature, also the electron transfer (ET) properties of ET proteins are influenced by pH-induced conformational changes.

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An overview of the solvent-driven aggregation of a series of chiral porphyrin derivatives studied by optical methods (UV/Vis, fluorescence, CD and RLS spectroscopies) is herein reported. The investigated porphyrins are characterized by the presence in the meso-positions of glycol-, steroidal- and glucosteroidal moieties, conferring amphiphilicity and solubility in aqueous media to the primarily hydrophobic porphyrin platform. Aggregation of the macrocycles is driven by a change in bulk solvent composition, forming architectures with supramolecular chirality, steered by the stereogenic centers on the porphyrin peripheral positions.

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Supported lipid membranes represent an elegant way to design a fluid interface able to mimic the physicochemical properties of biological membranes, with potential biotechnological applications. In this work, a diacyl phospholipid, the 1,2-dipalmitoyl-sn-glycero-3-phosphothioethanol (DPPTE), functionalized with a thiol group, was immobilized on a gold surface. In this molecule, the thiol group, responsible for the Au-S bond (45 kJ/mol) is located on the phospholipid polar head, letting the hydrophobic chain protrude from the film.

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The aggregation of a steroid-functionalised porphyrin derivative occurs with the formation of J-type chiral species. Spectroscopic and SEM studies indicate that the initial concentration of the macrocycle strongly influences the morphology of the final mesoscopic structures, as a consequence of a change in the mechanistic course of the self-assembly process. Fibrillar structures are obtained at low porphyrin concentration, whereas aggregates of globular shapes are formed on increasing the substrate concentration.

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The elusive, multiple fully extended (2.0(5) -helix) peptide conformation was searched with a series of C(α,α) -diethylglycine homo-oligomers (n = 1 to 5) functionalized by an electron transfer (ET) donor···acceptor (D···A) pair in acetonitrile and chloroform solutions. In the former solvent, all peptides investigated were shown to populate the 3(10) -helix conformation, whereas in chloroform the two shortest members of the series (n = 1 and n = 2) adopt predominantly the 2.

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New types of steroid-porphyrin conjugates derived from 20-hydroxyecdysone (20E) and 24-epibrassinolide (EBl) were synthesized. An exceptional regioselectivity in the reaction of both steroids with porphyrin boronic acids was found to give side-chain-conjugated boronic esters as sole products. UV-Vis-, fluorescence and NMR spectroscopy yielded similar data for all the studied compounds confirming the solvent driven supramolecular assembly with formation of J-aggregates.

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