The Experts below are selected from a list of 122865 Experts worldwide ranked by ideXlab platform
Giovanni Gallo - One of the best experts on this subject based on the ideXlab platform.
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identification of novel cryptic multifunctional antimicrobial peptides from the human stomach enabled by a computational Experimental Platform
ACS Synthetic Biology, 2018Co-Authors: Katia Pane, Valeria Cafaro, Angela Avitabile, Marcelo Der Torossian Torres, Adriana Vollaro, Eliana De Gregorio, Maria Rosaria Catania, Antimo Di Maro, Andrea Bosso, Giovanni GalloAbstract:Novel approaches are needed to combat antibiotic resistance. Here, we describe a computational–Experimental framework for the discovery of novel cryptic antimicrobial peptides (AMPs). The computational Platform, based on previously validated antimicrobial scoring functions, indicated the activation peptide of pepsin A, the main human stomach protease, and its N- and C-terminal halves as antimicrobial peptides. The three peptides from pepsinogen A3 isoform were prepared in a recombinant form using a fusion carrier specifically developed to express toxic peptides in Escherichia coli. Recombinant pepsinogen A3-derived peptides proved to be wide-spectrum antimicrobial agents with MIC values in the range 1.56–50 μM (1.56–12.5 μM for the whole activation peptide). Moreover, the activation peptide was bactericidal at pH 3.5 for relevant foodborne pathogens, suggesting that this new class of previously unexplored AMPs may contribute to microbial surveillance within the human stomach. The peptides showed no toxici...
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Identification of Novel Cryptic Multifunctional Antimicrobial Peptides from the Human Stomach Enabled by a Computational–Experimental Platform
2018Co-Authors: Katia Pane, Valeria Cafaro, Angela Avitabile, Marcelo Der Torossian Torres, Adriana Vollaro, Eliana De Gregorio, Maria Rosaria Catania, Antimo Di Maro, Andrea Bosso, Giovanni GalloAbstract:Novel approaches are needed to combat antibiotic resistance. Here, we describe a computational–Experimental framework for the discovery of novel cryptic antimicrobial peptides (AMPs). The computational Platform, based on previously validated antimicrobial scoring functions, indicated the activation peptide of pepsin A, the main human stomach protease, and its N- and C-terminal halves as antimicrobial peptides. The three peptides from pepsinogen A3 isoform were prepared in a recombinant form using a fusion carrier specifically developed to express toxic peptides in Escherichia coli. Recombinant pepsinogen A3-derived peptides proved to be wide-spectrum antimicrobial agents with MIC values in the range 1.56–50 μM (1.56–12.5 μM for the whole activation peptide). Moreover, the activation peptide was bactericidal at pH 3.5 for relevant foodborne pathogens, suggesting that this new class of previously unexplored AMPs may contribute to microbial surveillance within the human stomach. The peptides showed no toxicity toward human cells and exhibited anti-infective activity in vivo, reducing by up to 4 orders of magnitude the bacterial load in a mouse skin infection model. These peptides thus represent a promising new class of antibiotics. We envision that computationally guided data mining approaches such as the one described here will lead to the discovery of antibiotics from previously unexplored sources
Katia Pane - One of the best experts on this subject based on the ideXlab platform.
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identification of novel cryptic multifunctional antimicrobial peptides from the human stomach enabled by a computational Experimental Platform
ACS Synthetic Biology, 2018Co-Authors: Katia Pane, Valeria Cafaro, Angela Avitabile, Marcelo Der Torossian Torres, Adriana Vollaro, Eliana De Gregorio, Maria Rosaria Catania, Antimo Di Maro, Andrea Bosso, Giovanni GalloAbstract:Novel approaches are needed to combat antibiotic resistance. Here, we describe a computational–Experimental framework for the discovery of novel cryptic antimicrobial peptides (AMPs). The computational Platform, based on previously validated antimicrobial scoring functions, indicated the activation peptide of pepsin A, the main human stomach protease, and its N- and C-terminal halves as antimicrobial peptides. The three peptides from pepsinogen A3 isoform were prepared in a recombinant form using a fusion carrier specifically developed to express toxic peptides in Escherichia coli. Recombinant pepsinogen A3-derived peptides proved to be wide-spectrum antimicrobial agents with MIC values in the range 1.56–50 μM (1.56–12.5 μM for the whole activation peptide). Moreover, the activation peptide was bactericidal at pH 3.5 for relevant foodborne pathogens, suggesting that this new class of previously unexplored AMPs may contribute to microbial surveillance within the human stomach. The peptides showed no toxici...
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Identification of Novel Cryptic Multifunctional Antimicrobial Peptides from the Human Stomach Enabled by a Computational–Experimental Platform
2018Co-Authors: Katia Pane, Valeria Cafaro, Angela Avitabile, Marcelo Der Torossian Torres, Adriana Vollaro, Eliana De Gregorio, Maria Rosaria Catania, Antimo Di Maro, Andrea Bosso, Giovanni GalloAbstract:Novel approaches are needed to combat antibiotic resistance. Here, we describe a computational–Experimental framework for the discovery of novel cryptic antimicrobial peptides (AMPs). The computational Platform, based on previously validated antimicrobial scoring functions, indicated the activation peptide of pepsin A, the main human stomach protease, and its N- and C-terminal halves as antimicrobial peptides. The three peptides from pepsinogen A3 isoform were prepared in a recombinant form using a fusion carrier specifically developed to express toxic peptides in Escherichia coli. Recombinant pepsinogen A3-derived peptides proved to be wide-spectrum antimicrobial agents with MIC values in the range 1.56–50 μM (1.56–12.5 μM for the whole activation peptide). Moreover, the activation peptide was bactericidal at pH 3.5 for relevant foodborne pathogens, suggesting that this new class of previously unexplored AMPs may contribute to microbial surveillance within the human stomach. The peptides showed no toxicity toward human cells and exhibited anti-infective activity in vivo, reducing by up to 4 orders of magnitude the bacterial load in a mouse skin infection model. These peptides thus represent a promising new class of antibiotics. We envision that computationally guided data mining approaches such as the one described here will lead to the discovery of antibiotics from previously unexplored sources
Stefano Gonella - One of the best experts on this subject based on the ideXlab platform.
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manipulating waves with lego bricks a versatile Experimental Platform for metamaterial architectures
Applied Physics Letters, 2015Co-Authors: Paolo Celli, Stefano GonellaAbstract:In this letter, we discuss a versatile, fully reconfigurable Experimental Platform for the investigation of phononic phenomena in metamaterial architectures. The approach revolves around the use of 3D laser vibrometry to reconstruct global and local wavefield features in specimens obtained through simple arrangements of LEGO® bricks on a thin baseplate. The agility by which it is possible to reconfigure the brick patterns into a nearly endless spectrum of topologies makes this an effective approach for rapid Experimental proof of concept, as well as a powerful didactic tool, in the arena of phononic crystals and metamaterials engineering. We use our Platform to provide a compelling visual illustration of important spatial wave manipulation effects (waveguiding and seismic isolation), and to elucidate fundamental dichotomies between Bragg-based and locally resonant bandgap mechanisms.
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manipulating waves with lego bricks a versatile Experimental Platform for metamaterial architectures
Applied Physics Letters, 2015Co-Authors: Paolo Celli, Stefano GonellaAbstract:In this letter, we discuss a versatile, fully reconfigurable Experimental Platform for the investigation of phononic phenomena in metamaterial architectures. The approach revolves around the use of 3D laser vibrometry to reconstruct global and local wavefield features in specimens obtained through simple arrangements of LEGO® bricks on a thin baseplate. The agility by which it is possible to reconfigure the brick patterns into a nearly endless spectrum of topologies makes this an effective approach for rapid Experimental proof of concept, as well as a powerful didactic tool, in the arena of phononic crystals and metamaterials engineering. We use our Platform to provide a compelling visual illustration of important spatial wave manipulation effects (waveguiding and seismic isolation), and to elucidate fundamental dichotomies between Bragg-based and locally resonant bandgap mechanisms.
Angela Avitabile - One of the best experts on this subject based on the ideXlab platform.
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identification of novel cryptic multifunctional antimicrobial peptides from the human stomach enabled by a computational Experimental Platform
ACS Synthetic Biology, 2018Co-Authors: Katia Pane, Valeria Cafaro, Angela Avitabile, Marcelo Der Torossian Torres, Adriana Vollaro, Eliana De Gregorio, Maria Rosaria Catania, Antimo Di Maro, Andrea Bosso, Giovanni GalloAbstract:Novel approaches are needed to combat antibiotic resistance. Here, we describe a computational–Experimental framework for the discovery of novel cryptic antimicrobial peptides (AMPs). The computational Platform, based on previously validated antimicrobial scoring functions, indicated the activation peptide of pepsin A, the main human stomach protease, and its N- and C-terminal halves as antimicrobial peptides. The three peptides from pepsinogen A3 isoform were prepared in a recombinant form using a fusion carrier specifically developed to express toxic peptides in Escherichia coli. Recombinant pepsinogen A3-derived peptides proved to be wide-spectrum antimicrobial agents with MIC values in the range 1.56–50 μM (1.56–12.5 μM for the whole activation peptide). Moreover, the activation peptide was bactericidal at pH 3.5 for relevant foodborne pathogens, suggesting that this new class of previously unexplored AMPs may contribute to microbial surveillance within the human stomach. The peptides showed no toxici...
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Identification of Novel Cryptic Multifunctional Antimicrobial Peptides from the Human Stomach Enabled by a Computational–Experimental Platform
2018Co-Authors: Katia Pane, Valeria Cafaro, Angela Avitabile, Marcelo Der Torossian Torres, Adriana Vollaro, Eliana De Gregorio, Maria Rosaria Catania, Antimo Di Maro, Andrea Bosso, Giovanni GalloAbstract:Novel approaches are needed to combat antibiotic resistance. Here, we describe a computational–Experimental framework for the discovery of novel cryptic antimicrobial peptides (AMPs). The computational Platform, based on previously validated antimicrobial scoring functions, indicated the activation peptide of pepsin A, the main human stomach protease, and its N- and C-terminal halves as antimicrobial peptides. The three peptides from pepsinogen A3 isoform were prepared in a recombinant form using a fusion carrier specifically developed to express toxic peptides in Escherichia coli. Recombinant pepsinogen A3-derived peptides proved to be wide-spectrum antimicrobial agents with MIC values in the range 1.56–50 μM (1.56–12.5 μM for the whole activation peptide). Moreover, the activation peptide was bactericidal at pH 3.5 for relevant foodborne pathogens, suggesting that this new class of previously unexplored AMPs may contribute to microbial surveillance within the human stomach. The peptides showed no toxicity toward human cells and exhibited anti-infective activity in vivo, reducing by up to 4 orders of magnitude the bacterial load in a mouse skin infection model. These peptides thus represent a promising new class of antibiotics. We envision that computationally guided data mining approaches such as the one described here will lead to the discovery of antibiotics from previously unexplored sources
Marcelo Der Torossian Torres - One of the best experts on this subject based on the ideXlab platform.
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identification of novel cryptic multifunctional antimicrobial peptides from the human stomach enabled by a computational Experimental Platform
ACS Synthetic Biology, 2018Co-Authors: Katia Pane, Valeria Cafaro, Angela Avitabile, Marcelo Der Torossian Torres, Adriana Vollaro, Eliana De Gregorio, Maria Rosaria Catania, Antimo Di Maro, Andrea Bosso, Giovanni GalloAbstract:Novel approaches are needed to combat antibiotic resistance. Here, we describe a computational–Experimental framework for the discovery of novel cryptic antimicrobial peptides (AMPs). The computational Platform, based on previously validated antimicrobial scoring functions, indicated the activation peptide of pepsin A, the main human stomach protease, and its N- and C-terminal halves as antimicrobial peptides. The three peptides from pepsinogen A3 isoform were prepared in a recombinant form using a fusion carrier specifically developed to express toxic peptides in Escherichia coli. Recombinant pepsinogen A3-derived peptides proved to be wide-spectrum antimicrobial agents with MIC values in the range 1.56–50 μM (1.56–12.5 μM for the whole activation peptide). Moreover, the activation peptide was bactericidal at pH 3.5 for relevant foodborne pathogens, suggesting that this new class of previously unexplored AMPs may contribute to microbial surveillance within the human stomach. The peptides showed no toxici...
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Identification of Novel Cryptic Multifunctional Antimicrobial Peptides from the Human Stomach Enabled by a Computational–Experimental Platform
2018Co-Authors: Katia Pane, Valeria Cafaro, Angela Avitabile, Marcelo Der Torossian Torres, Adriana Vollaro, Eliana De Gregorio, Maria Rosaria Catania, Antimo Di Maro, Andrea Bosso, Giovanni GalloAbstract:Novel approaches are needed to combat antibiotic resistance. Here, we describe a computational–Experimental framework for the discovery of novel cryptic antimicrobial peptides (AMPs). The computational Platform, based on previously validated antimicrobial scoring functions, indicated the activation peptide of pepsin A, the main human stomach protease, and its N- and C-terminal halves as antimicrobial peptides. The three peptides from pepsinogen A3 isoform were prepared in a recombinant form using a fusion carrier specifically developed to express toxic peptides in Escherichia coli. Recombinant pepsinogen A3-derived peptides proved to be wide-spectrum antimicrobial agents with MIC values in the range 1.56–50 μM (1.56–12.5 μM for the whole activation peptide). Moreover, the activation peptide was bactericidal at pH 3.5 for relevant foodborne pathogens, suggesting that this new class of previously unexplored AMPs may contribute to microbial surveillance within the human stomach. The peptides showed no toxicity toward human cells and exhibited anti-infective activity in vivo, reducing by up to 4 orders of magnitude the bacterial load in a mouse skin infection model. These peptides thus represent a promising new class of antibiotics. We envision that computationally guided data mining approaches such as the one described here will lead to the discovery of antibiotics from previously unexplored sources
