Publications by authors named "Michael Quagliata"

There are still no linear antimicrobial peptides (AMPs) available as a treatment option against bacterial infections. This is caused by several drawbacks that come with AMPs such as limited proteolytic stability and low selectivity against human cells. In this work, we screened a small library of rationally designed new peptides based on the cell-penetrating peptide sC18* toward their antimicrobial activity.

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A gel that exhibits intrinsically multiple-responsive behavior was prepared from an oligopeptide and studied. ACP(65-74) is an active decapeptide fragment of acyl carrier protein. We investigated 3% w/v ACP(65-74)-NH self-healing physical gels in water, glycerol carbonate (GC), and their mixtures.

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Introduction: Thymosins are small proteins found mainly in the thymus. They are involved in several biological processes, including immunoregulation, angiogenesis, and anti-inflammatory activity. Due to these multiple activities, thymosins are widely used as therapeutics.

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To date, the severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) COVID-19 pandemic continues to be a potentially lethal disease. Although both vaccines and specific antiviral drugs have been approved, the search for more specific therapeutic approaches is still ongoing. The infection mechanism of SARS-CoV-2 consists of several stages, and each one can be selectively blocked to disrupt viral infection.

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Severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has posed a great concern in human population. To fight coronavirus emergence, we have dissected the conserved amino acid region of the internal fusion peptide in the S2 subunit of Spike glycoprotein of SARS-CoV-2 to design new inhibitory peptides. Among the 11 overlapping peptides (9-23-mer), PN19, a 19-mer peptide, exhibited a powerful inhibitory activity against different SARS-CoV-2 clinical isolate variants in absence of cytotoxicity.

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Despite the availability of vaccines, COVID-19 continues to be aggressive, especially in immunocompromised individuals. Therefore, the development of a specific therapeutic agent with antiviral activity against SARS-CoV-2 is necessary. The infection pathway starts when the of the viral spike protein interacts with the (ACE2), which acts as a host receptor for the RBD expressed on the host cell surface.

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Introduction: Eradication of malaria remains one of the main aims of medicine. Despite progress in malaria treatment, mortality rate remains high, especially in the poorest parts of the world. Therefore, prevention through vaccines is fundamental and recent approval of the first effective vaccine reinforced this assumption.

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Article Synopsis
  • Multiple sclerosis (MS) is an autoimmune disorder characterized by inflammation and the damaging of myelin due to antibody activity.
  • Researchers created two glucosylated peptides from human myelin proteins, which possess similar structures to a specific antigen recognized by MS patient antibodies, to study their immune response.
  • The findings indicate that these peptides are recognized by antibodies in MS patients and share immunological similarities with both human and bacterial proteins, suggesting a possible link between these proteins that might contribute to the onset of MS.
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Peptide fragments of glycoproteins containing multiple -glycosylated sites are essential biochemical tools not only to investigate protein-protein interactions but also to develop glycopeptide-based diagnostics and immunotherapy. However, solid-phase synthesis of glycopeptides containing multiple -glycosylated sites is hampered by difficult couplings, which results in a substantial drop in yield. To increase the final yield, large amounts of reagents but also time-consuming steps are required.

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Article Synopsis
  • The study focuses on Myelin Basic Protein (MBP) and its role in Multiple Sclerosis, particularly how its α-helix structure affects antibody recognition.
  • Researchers synthesized and tested two different lengths of MBP peptides, finding that elongating the peptide improves antibody recognition but destabilizes its helical structure.
  • Results indicate that the original shorter peptide (MBP 81-106) is better recognized by IgM antibodies in competitive ELISA due to its stable helical form, highlighting the complexity of antibody-antigen interactions in different testing conditions.
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