Publications by authors named "Marco Balestrieri"

Antimicrobial peptides (AMPs) are considered an attractive generation of novel antibiotics due to their advantageous properties such as a broad spectrum of antimicrobial activity against pathogens, low cytotoxicity, and drug resistance. Although they have common structural features and it has been widely demonstrated that bacterial membranes represent the main target of the peptide activity, the exact mechanism underlying the membrane perturbation by AMPs is not fully understood. Nevertheless, all the proposed modes of action implicate the preliminary interaction of AMPs with the negatively charged lipids in bacterial membranes.

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Introduction: The aim of the study was to define a core outcome set (COS) to be measured following cataract surgery for the postoperative evaluation of monofocal intraocular lenses (IOLs). Compared to current COSs, the present work provides updates considering the advances in the technology due to the development of new generation monofocal IOLs, which are characterized by a safety profile comparable to standard monofocal IOLs but with an extended range of intermediate vision.

Methods: Healthcare professionals (ophthalmologist surgeons) and patients were involved in the selection of outcomes to be included in the COS, starting from a list of indicators retrieved from a systematic literature search.

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Antimicrobial activity of many AMPs can be improved by lysine-to-arginine substitution due to a more favourable interaction of arginine guanidinium moiety with bacterial membranes. In a previous work, the structural and functional characterization of an amphipathic antimicrobial peptide named RiLK1, including lysine and arginine as the positively charged amino acids in its sequence, was reported. Specifically, RiLK1 retained its β-sheet structure under a wide range of environmental conditions (temperature, pH, and ionic strength), and exhibited bactericidal activity against Gram-positive and Gram-negative bacteria and fungal pathogens with no evidence of toxicity on mammalian cells.

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Peroxidases are widespread key antioxidant enzymes that catalyse the oxidation of electron donor substrates in parallel with the decomposition of HO. In this work, a novel tomato peroxidase, named SAAP2, was isolated from MicroTom cell cultures, purified, and characterised. The enzyme was identified with 64% sequence coverage as the leprx21 gene product (suberization-associated anionic peroxidase 2-like) from Solanum lycopersicum, 334 amino acids long.

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Fresh fish are highly perishable, owing mainly to their moisture content, high amount of free amino acids and polyunsaturated fatty acids. Microorganisms and chemical reactions cause the spoilage, leading to loss in quality, human health risks and a market value reduction. Therefore, the fishing industry has always been willing to explore new technologies to increase quality and safety of fish products through a decrease of the microbiological and biochemical damage.

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Antimicrobial peptides (AMPs) represent a skilled class of new antibiotics, due to their broad range of activity, rapid killing, and low bacterial resistance. Many efforts have been made to discover AMPs with improved performances, i.e.

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Background: Hepatitis C Virus (HCV) infection represents a global problem, and it is related to both hepatic and extra-hepatic manifestations (e.g., xerophthalmia).

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Antimicrobial peptides (AMPs) are excellent candidates to fight multi-resistant pathogens worldwide and are considered promising bio-preservatives to control microbial spoilage through food processing. To date, designing de novo AMPs with high therapeutic indexes, low-cost synthesis, high resistance, and bioavailability, remains a challenge. In this study, a novel decapeptide, named RiLK1, was rationally designed starting from the sequence of the previously characterized AMP 1018-K6, with the aim of developing short peptides, and promoting higher selectivity over mammalian cells, antibacterial activity, and structural resistance under different salt, pH, and temperature conditions.

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is a well-known and important medicinal plant, with a long history of traditional medicine use. Several studies showed that it contains many bioactive compounds with a wide range of pharmacological effects. In light of these past researches, were chosen to consider its potential antimicrobial action.

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Fresh products are characterized by reduced shelf-life because they are an excellent growth medium for a lot of microorganisms. Therefore, the microbial spoilage causing significant food supply losses has become an enormous economic and ethical problem worldwide. The antimicrobial packaging is offering a viable solution to tackle this economic and safety issue by extending the shelf-life and improving the quality and safety of fresh products.

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An overproduction of free radicals or reactive oxygen species, often due to environmental factors, can alter the DNA structure and irreversibly modify proteins and lipids in the living cells. The superoxide anion (O) is one of the strongest oxidant molecules produced under oxidative stress conditions but it can be neutralized by the action of the enzymes SuperOxide Dismutases (SODs). In all the human tissues, SODs are essential for the prevention of serious diseases and the protection against oxidative stress damages.

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Aims: To evaluate deep corneal densitometry and visual outcomes after big-bubble (BB-DALK) and visco-bubble (VB-DALK) deep anterior lamellar keratoplasty performed in patients with keratoconus.

Methods: Prospective comparative study of 50 advanced keratoconic patients who underwent DALK surgery; 25 eyes (group I) were completed with BB-DALK and 25 eyes (group II) with VB-DALK after the failure of pneumatic dissection. Best spectacle-corrected visual acuity (BSCVA), corneal tomographic parameters and endothelial cell count were recorded 1, 3, 6, 12 and 24 months after surgery.

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Food packaging is not only a simple protective barrier, but a real "active" component, which is expected to preserve food quality, safety and shelf-life. Therefore, the materials used for packaging production should show peculiar features and properties. Specifically, antimicrobial packaging has recently gained great attention with respect to both social and economic impacts.

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Synthetic antibacterial peptides are advanced weapons that scientists design and produce to confront current threats of harmful and mortal pathogens, which could affect humans in everyday life. Recently, many small amino acid sequences, greatly efficient in their antibacterial action, have been reported in the literature. To date, only a few synthetic peptides, acting at micromolar or even tenths of micromolar concentrations, are on the market as commercial products, mainly because of their high cost of production.

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Antimicrobial peptides have received great attention for their potential benefits to extend the shelf-life of food-products. Innate defense regulator peptide-1018 (IDR-1018) represents a promising candidate for such applications, due to its broad-spectrum antimicrobial activity, although food-isolated pathogens have been poorly investigated. Herein, we describe the design and the structural-functional characterization of a new 1018-derivative peptide named 1018-K6, in which the alanine in position 6 was replaced with a lysine.

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Alzheimer's disease (AD) is a progressive, multifactorial neurodegenerative disorder that is the main cause of dementia. To date, there are no definitive diagnostic tests that can predict or assess onset and progression of the disease. Blood biomarkers for AD are being sought for many years but their identification remains a challenging task.

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We describe the use of a simple tool to evaluate the postoperative alignment of toric intraocular lenses (IOLs). The entire anterior segment is scanned using anterior segment optical coherence tomography and analyzed with an internal dedicated tool. A topographic map is displayed along with an anterior segment image, including a linear axis marker centered on the corneal apex.

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The oxidative challenge represents an important factor affecting the adaptive strategies in Antarctic fish, but their impact on the protein degradation machinery still remains unclear. The previous analysis of the first 26S proteasome from the Antarctic red-blooded fish , evidenced improved antioxidant functions necessary to counteract the environmental pro-oxidant conditions. The purpose of this work was to carry out a study on 26S proteasomes from the temperate red-blooded and the icefish in comparison with the isoform already described from , to better elucidate the cold-adapted physiological functions of this complex.

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The proteasome is a multienzymatic complex that controls the half-life of the majority of intracellular proteins, including those involved in apoptosis and cell-cycle progression. Recently, proteasome inhibition has been shown to be an effective anticancer strategy, although its downregulation is often accompanied by severe undesired side effects. We previously reported that the inhibition of acylpeptide hydrolase (APEH) by the peptide SsCEI 4 can significantly affect the proteasome activity in A375 melanoma or Caco-2 adenocarcinoma cell lines, thus shedding new light on therapeutic strategies based on downstream regulation of proteasome functions.

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Here we report details on the design and conformational analysis of two novel peptides showing antimicrobial properties, as reported in the research article, "New antimicrobial peptides against foodborne pathogens: from in silico design to experimental evidence" G. Palmieri, M. Balestrieri, Y.

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Recently there has been growing interest in the discovery of new antimicrobial agents to increase safety and shelf-life of food products. Here, we developed an innovative approach by introducing the concept that mitochondrial targeting peptides (MTP) can interact and disrupt bacterial membranes, acting as antimicrobial agents. As proof-of-principle, we used a multidisciplinary strategy by combining in silico predictions, docking simulations and antimicrobial assays, to identify two peptides, MTP1 and MTP2, which were structurally and functionally characterized.

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Protein homoeostasis is a fundamental process allowing the preservation of functional proteins and it has a great impact on the life of the Antarctic organisms. However, the effect of low temperatures on protein turnover is poorly understood and the cold-adaptation of the degradation machinery remains an unresolved issue. As the 26S proteasome represents the main proteolytic system devoted to the controlled degradation of intracellular proteins, the purpose of the present study was to investigate the functions of this complex in the notothenioid Trematomus bernacchii, in order to better understand its role in the physiology of Antarctic fish.

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Acylpeptide hydrolase (APEH) is a ubiquitous cytosolic protease that plays an important role in the detoxification of oxidised proteins. In this work, to further explore the physiological role of this enzyme, two apeh cDNAs were isolated from the Chionodraco hamatus icefish, which lives in the highly oxygenated Antarctic marine environment. The encoded proteins (APEH-1(Ch) and APEH-2(Ch)) were characterised in comparison with the uniquely expressed isoform from the temperate fish Dicentrarchus labrax (APEH-1Dl) and the two APEHs from the red-blooded Antarctic fish Trematomus bernacchii (APEH-1(Tb) and APEH-2(Tb)).

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Purpose: To evaluate the efficacy of 2 dexamethasone intravitreal implants and 1 ranibizumab intravitreal injection after a bilateral postoperative complication of cataract surgery as pseudophakic cystoid macular edema.

Patients And Methods: A 70-year-old male patient with systemic hypertension developed a progressive cystoid macular edema (CME) in both eyes starting between 10 and 20 days after cataract surgery. Two intravitreal dexamethasone implants and 1 ranibizumab injection were administered; first in the right eye (RE) and then in the left eye (LE).

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