Publications by authors named "I C M Fensterseifer"

Article Synopsis
  • - Defensins are found in various organisms and categorized into - and -defensins; recent studies have identified 74 new -defensins in bacteria and propose a new classification system for them.
  • - The study presents the first NMR structure of a defensin known as Xanthusin-1, suggesting it may represent a unique group of defensins, with gene expression observed in specific growth media.
  • - Findings indicate a broader distribution of defensins beyond eukaryotes, hinting at a prokaryotic origin for certain motifs, and show that both Gram-positive and Gram-negative bacteria possess defensins, indicating early evolutionary roots but also significant gene loss.
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Bacterial resistance is a threat to health worldwide, mainly due to reduced effective treatment. In this context, the search for strategies to control such infections and suppress antimicrobial resistance is necessary. One of the strategies that has been used is combination therapy.

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Discovering antibiotic molecules able to hold the growing spread of antimicrobial resistance is one of the most urgent endeavors that public health must tackle. The case of Gram-negative bacterial pathogens is of special concern, as they are intrinsically resistant to many antibiotics, due to an outer membrane that constitutes an effective permeability barrier. Antimicrobial peptides (AMPs) have been pointed out as potential alternatives to conventional antibiotics, as their main mechanism of action is membrane disruption, arguably less prone to elicit resistance in pathogens.

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Novel antibiotics are urgently needed to combat multidrug-resistant pathogens. Venoms represent previously untapped sources of novel drugs. Here we repurposed mastoparan-L, the toxic active principle derived from the venom of the wasp , into synthetic antimicrobials.

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Tetracycline (TC), oxytetracycline (OTC), and chlortetracycline (CTC) interactions with the allergenic milk protein casein (CAS) were here evaluated simulating food conditions. The antibiotics assessed interact with CAS through static quenching and form non-fluorescent complexes. At 30 °C, the binding constant (K) varied from 0.

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