The Experts below are selected from a list of 18 Experts worldwide ranked by ideXlab platform
Emilio Montesinos - One of the best experts on this subject based on the ideXlab platform.
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production of bp178 a Derivative of the synthetic antibacterial peptide bp100 in the rice seed endosperm
BMC Plant Biology, 2017Co-Authors: Laura Montesinos, Mireia Bundo, Esther Badosa, Blanca San Segundo, Maria Coca, Emilio MontesinosAbstract:BP178 peptide is a synthetic BP100-Magainin Derivative possessing strong inhibitory activity against plant pathogenic bacteria, offering a great potential for future applications in plant protection and other fields. Here we report the production and recovery of a bioactive BP178 peptide using rice seeds as biofactories. A synthetic gene encoding the BP178 peptide was prepared and introduced in rice plants. The gene was efficiently expressed in transgenic rice under the control of an endosperm-specific promoter. Among the three endosperm-specific rice promoters (Glutelin B1, Glutelin B4 or Globulin 1), best results were obtained when using the Globulin 1 promoter. The BP178 peptide accumulated in the seed endosperm and was easily recovered from rice seeds using a simple procedure with a yield of 21 μg/g. The transgene was stably inherited for at least three generations, and peptide accumulation remained stable during long term storage of transgenic seeds. The purified peptide showed in vitro activity against the bacterial plant pathogen Dickeya sp., the causal agent of the dark brown sheath rot of rice. Seedlings of transgenic events showed enhanced resistance to the fungal pathogen Fusarium verticillioides, supporting that the in planta produced peptide was biologically active. The strategy developed in this work for the sustainable production of BP178 peptide using rice seeds as biofactories represents a promising system for future production of peptides for plant protection and possibly in other fields.
Samuel H Gellman - One of the best experts on this subject based on the ideXlab platform.
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mimicry of host defense peptides by unnatural oligomers antimicrobial β peptides
Journal of the American Chemical Society, 2002Co-Authors: Emilie A Porter, Bernard Weisblum, Samuel H GellmanAbstract:We have designed β-amino acid oligomers that are helical, cationic, and amphiphilic with the intention of mimicking the biological activity of amphiphilic, cationic α-helical antimicrobial peptides found in nature (e.g., Magainins). We have previously identified a 17-residue β-peptide (called β-17) with antibiotic activity similar to that of a Magainin Derivative against four bacterial species, including two clinical isolates that are resistant to common antibiotics. This β-peptide displays very low hemolytic activity against human red blood cells, which indicates selectivity for bacterial cells over mammalian cells. Here we examine some of the factors important for activity in this class of β-peptides. An amphiphilic helix is necessary, because a nonamphiphilic isomer proved to be inactive. The ratio of cationic to hydrophobic residues is also important. Active β-peptides induce the leakage of β-galactosidase from treated Bacillus subtilis cells, as do α-helical antibiotic peptides, and this similarity s...
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non haemolytic β amino acid oligomers
Nature, 2000Co-Authors: Emilie A Porter, Xifang Wang, Heeseung Lee, Bernard Weisblum, Samuel H GellmanAbstract:Pathogenic bacteria are becoming increasingly resistant to common antibiotics, stimulating an intensive search for new ones. Knowing that a class of medium-sized peptides (Magainins1) are widely used by host organisms as a defence against microbial invasion2, we developed a β-amino-acid oligomer (β-peptide) that mimics these natural antibiotics and tested it for antimicrobial activity. We find not only that the activity of our β-peptide is comparable to that of a Magainin Derivative but also that it is effective against four bacterial species, including two pathogens that are resistant to common antibiotics.
Laura Montesinos - One of the best experts on this subject based on the ideXlab platform.
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production of bp178 a Derivative of the synthetic antibacterial peptide bp100 in the rice seed endosperm
BMC Plant Biology, 2017Co-Authors: Laura Montesinos, Mireia Bundo, Esther Badosa, Blanca San Segundo, Maria Coca, Emilio MontesinosAbstract:BP178 peptide is a synthetic BP100-Magainin Derivative possessing strong inhibitory activity against plant pathogenic bacteria, offering a great potential for future applications in plant protection and other fields. Here we report the production and recovery of a bioactive BP178 peptide using rice seeds as biofactories. A synthetic gene encoding the BP178 peptide was prepared and introduced in rice plants. The gene was efficiently expressed in transgenic rice under the control of an endosperm-specific promoter. Among the three endosperm-specific rice promoters (Glutelin B1, Glutelin B4 or Globulin 1), best results were obtained when using the Globulin 1 promoter. The BP178 peptide accumulated in the seed endosperm and was easily recovered from rice seeds using a simple procedure with a yield of 21 μg/g. The transgene was stably inherited for at least three generations, and peptide accumulation remained stable during long term storage of transgenic seeds. The purified peptide showed in vitro activity against the bacterial plant pathogen Dickeya sp., the causal agent of the dark brown sheath rot of rice. Seedlings of transgenic events showed enhanced resistance to the fungal pathogen Fusarium verticillioides, supporting that the in planta produced peptide was biologically active. The strategy developed in this work for the sustainable production of BP178 peptide using rice seeds as biofactories represents a promising system for future production of peptides for plant protection and possibly in other fields.
Emilie A Porter - One of the best experts on this subject based on the ideXlab platform.
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mimicry of host defense peptides by unnatural oligomers antimicrobial β peptides
Journal of the American Chemical Society, 2002Co-Authors: Emilie A Porter, Bernard Weisblum, Samuel H GellmanAbstract:We have designed β-amino acid oligomers that are helical, cationic, and amphiphilic with the intention of mimicking the biological activity of amphiphilic, cationic α-helical antimicrobial peptides found in nature (e.g., Magainins). We have previously identified a 17-residue β-peptide (called β-17) with antibiotic activity similar to that of a Magainin Derivative against four bacterial species, including two clinical isolates that are resistant to common antibiotics. This β-peptide displays very low hemolytic activity against human red blood cells, which indicates selectivity for bacterial cells over mammalian cells. Here we examine some of the factors important for activity in this class of β-peptides. An amphiphilic helix is necessary, because a nonamphiphilic isomer proved to be inactive. The ratio of cationic to hydrophobic residues is also important. Active β-peptides induce the leakage of β-galactosidase from treated Bacillus subtilis cells, as do α-helical antibiotic peptides, and this similarity s...
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non haemolytic β amino acid oligomers
Nature, 2000Co-Authors: Emilie A Porter, Xifang Wang, Heeseung Lee, Bernard Weisblum, Samuel H GellmanAbstract:Pathogenic bacteria are becoming increasingly resistant to common antibiotics, stimulating an intensive search for new ones. Knowing that a class of medium-sized peptides (Magainins1) are widely used by host organisms as a defence against microbial invasion2, we developed a β-amino-acid oligomer (β-peptide) that mimics these natural antibiotics and tested it for antimicrobial activity. We find not only that the activity of our β-peptide is comparable to that of a Magainin Derivative but also that it is effective against four bacterial species, including two pathogens that are resistant to common antibiotics.
Blanca San Segundo - One of the best experts on this subject based on the ideXlab platform.
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production of bp178 a Derivative of the synthetic antibacterial peptide bp100 in the rice seed endosperm
BMC Plant Biology, 2017Co-Authors: Laura Montesinos, Mireia Bundo, Esther Badosa, Blanca San Segundo, Maria Coca, Emilio MontesinosAbstract:BP178 peptide is a synthetic BP100-Magainin Derivative possessing strong inhibitory activity against plant pathogenic bacteria, offering a great potential for future applications in plant protection and other fields. Here we report the production and recovery of a bioactive BP178 peptide using rice seeds as biofactories. A synthetic gene encoding the BP178 peptide was prepared and introduced in rice plants. The gene was efficiently expressed in transgenic rice under the control of an endosperm-specific promoter. Among the three endosperm-specific rice promoters (Glutelin B1, Glutelin B4 or Globulin 1), best results were obtained when using the Globulin 1 promoter. The BP178 peptide accumulated in the seed endosperm and was easily recovered from rice seeds using a simple procedure with a yield of 21 μg/g. The transgene was stably inherited for at least three generations, and peptide accumulation remained stable during long term storage of transgenic seeds. The purified peptide showed in vitro activity against the bacterial plant pathogen Dickeya sp., the causal agent of the dark brown sheath rot of rice. Seedlings of transgenic events showed enhanced resistance to the fungal pathogen Fusarium verticillioides, supporting that the in planta produced peptide was biologically active. The strategy developed in this work for the sustainable production of BP178 peptide using rice seeds as biofactories represents a promising system for future production of peptides for plant protection and possibly in other fields.
