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Antibacterial activity of short cationic model peptides
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Special Abstracts / Journal of Biotechnology 150S (2010) S1–S576
bacteria. Peptides of other type of secondary structure showed insignificant antimicrobial activity. By understanding the relationship between peptide structure and function, as well as their mechanism of action, we can define a basic set of conformational requirements necessary for designing potent antimicrobial peptide agents that will aid in improving animal and human health and agricultural and food supplies. doi:10.1016/j.jbiotec.2010.09.010 [P-C.45] A new technology for fast multiplexed immunoassays A.D. Edwards 1,∗ , N. Reis 1 , M. Mackley 2 , N.K.H. Slater 2 1
University of Cambridge, United Kingdom University of Reading, United Kingdom Keywords: Immunoassay; Multiplex Immunoassay; diagnostic; point of care immunoassay 2
doi:10.1016/j.jbiotec.2010.09.009 [P-C.44] Antibacterial activity of short cationic model peptides Fanny Guzman 1,∗ , Sergio Marshall 1,2 , Conztanza Cardenas 1 , Gloria Arenas 4 , Luis Mercado 1 , Fernando Albericio 3 1
Laboratory of Genetics and Molecular Immunology, Institute of Biology and Biotechnology Nucleus Pontificia Universidad Católica de Valparaíso;, Chile 2 Regional Center for Health Food Research (CREAS), Chile 3 Department of Organic Chemistry, Universitat de Barcelona, Spain 4 School of Food Technology Pontificia Universidad Católica de Valparaís, Chile Keywords: Antimicrobial peptides; Homopeptides; Structure and function; Cationic peptides
Short cationic peptides are a particularly abundant and widespread class of antimicrobial agents. However, it is not yet clear why some peptides are active against one particular bacterial strain but not against others. Due to their relatively small size they can be conveniently produced by solid-phase synthesis, which allows generating a substantial amount of data about structure-activity relationship. Since lysine and arginine are the preferred residues at several positions of such peptides, we synthesized and investigated 7, 14 and 21 homopeptides of lysine and arginine by developing a strategy of solid-phase synthesis and purified them to a level higher than 95% by reverse-phase high pressure liquid chromatography. The designed sequence was confirmed by mass spectroscopy. Antibacterial effects of all synthesized homopeptides were evaluated by broth and solid dilution assay on a range of pathogens. The Minimum Inhibitory Concentration (MIC) and the Minimum Bactericidal Concentration (MBC) of peptides were determined on E. coli, L. monocytogenes, S. typhii, S. epidermis and S. aureus cells. The lysine homopeptide composed of 14 residues exhibited the highest antimicrobial activity of all studied. Arginine homopeptides did not show significant antimicrobial activity. Structural characterization by circular dichroism spectroscopy demonstrated that the 14 homolysine peptide adopts a polyproline II (PPII) conformation. However, the high hydrophobicity of the lysine side chains (higher than arginine), combined with a stabilized PPII structure conferred enhanced inhibition on
Immunoassays are the most powerful tool of detection of specific substances in biological samples for a wide range of healthcare applications ranging from cancer and cardiovascular biomarker measurement to infectious disease detection. There is a rapidly growing need to simultaneously measure multiple specific analytes within a single complex sample, a technique known as multiplex immunoassay. We have invented a new, simple technology that conducts standard enzyme-linked immunoassay assays within a plastic film device, allowing rapid and simultaneous quantitative detection of 10 or more analytes in multiple samples. The new technology interfaces with current liquid handling laboratory equipment (multichannel pipettes) and a colorimetric signal is detected with low-cost optical devices, such as a consumer flatbed scanner. The device is manufactured using a patented costefficient process and allows faster and easier multiplexed detection than standard assays whilst presenting similar sensitivities as demonstrated by proof-of-concept experiments. The new technology is being further explored as the basis for a portable multiplex immunoassay toolkit for a broad array of applications from lowcost point-of-care healthcare to biosecurity. doi:10.1016/j.jbiotec.2010.09.011 [P-C.46] BIOLIP, a biotechnology-oriented database of oil content in plants, algae, fungi and cyanobacteria A. Papini 1,∗ , S. Mosti 1 , P. Lio’ 2 , S. Haider 2 1
University of Florence, Italy University of Cambridge, United Kingdom Keywords: Fatty acids; Algae; Cyanobacteria; Lipid database 2
Lipids are an essential category of organic substances of interest in industrial fields, as biofuels (as alternatives to fossil fuels), biomasses for biotechnological uses and as health-related compounds. The main lipid sources are angiosperms species as Brassicaceae, soy, maize, oil palm and Jatropha. New crops are studied in order to obtain new varieties for with better yield, water and environmental necessities. Recently eukaryotic algae and cyanobacteria (Schenk et al., 2008) have been investigated to obtain lipids sources to increase productivity and to reduce the conflict with food cultivations. Our database BIOLIP (www.lipidresource.eu/biolip) aims to collect data on lipid content of organisms, with a biotechnology-
Special Abstracts / Journal of Biotechnology 150S (2010) S1–S576
bacteria. Peptides of other type of secondary structure showed insignificant antimicrobial activity. By understanding the relationship between peptide structure and function, as well as their mechanism of action, we can define a basic set of conformational requirements necessary for designing potent antimicrobial peptide agents that will aid in improving animal and human health and agricultural and food supplies. doi:10.1016/j.jbiotec.2010.09.010 [P-C.45] A new technology for fast multiplexed immunoassays A.D. Edwards 1,∗ , N. Reis 1 , M. Mackley 2 , N.K.H. Slater 2 1
University of Cambridge, United Kingdom University of Reading, United Kingdom Keywords: Immunoassay; Multiplex Immunoassay; diagnostic; point of care immunoassay 2
doi:10.1016/j.jbiotec.2010.09.009 [P-C.44] Antibacterial activity of short cationic model peptides Fanny Guzman 1,∗ , Sergio Marshall 1,2 , Conztanza Cardenas 1 , Gloria Arenas 4 , Luis Mercado 1 , Fernando Albericio 3 1
Laboratory of Genetics and Molecular Immunology, Institute of Biology and Biotechnology Nucleus Pontificia Universidad Católica de Valparaíso;, Chile 2 Regional Center for Health Food Research (CREAS), Chile 3 Department of Organic Chemistry, Universitat de Barcelona, Spain 4 School of Food Technology Pontificia Universidad Católica de Valparaís, Chile Keywords: Antimicrobial peptides; Homopeptides; Structure and function; Cationic peptides
Short cationic peptides are a particularly abundant and widespread class of antimicrobial agents. However, it is not yet clear why some peptides are active against one particular bacterial strain but not against others. Due to their relatively small size they can be conveniently produced by solid-phase synthesis, which allows generating a substantial amount of data about structure-activity relationship. Since lysine and arginine are the preferred residues at several positions of such peptides, we synthesized and investigated 7, 14 and 21 homopeptides of lysine and arginine by developing a strategy of solid-phase synthesis and purified them to a level higher than 95% by reverse-phase high pressure liquid chromatography. The designed sequence was confirmed by mass spectroscopy. Antibacterial effects of all synthesized homopeptides were evaluated by broth and solid dilution assay on a range of pathogens. The Minimum Inhibitory Concentration (MIC) and the Minimum Bactericidal Concentration (MBC) of peptides were determined on E. coli, L. monocytogenes, S. typhii, S. epidermis and S. aureus cells. The lysine homopeptide composed of 14 residues exhibited the highest antimicrobial activity of all studied. Arginine homopeptides did not show significant antimicrobial activity. Structural characterization by circular dichroism spectroscopy demonstrated that the 14 homolysine peptide adopts a polyproline II (PPII) conformation. However, the high hydrophobicity of the lysine side chains (higher than arginine), combined with a stabilized PPII structure conferred enhanced inhibition on
Immunoassays are the most powerful tool of detection of specific substances in biological samples for a wide range of healthcare applications ranging from cancer and cardiovascular biomarker measurement to infectious disease detection. There is a rapidly growing need to simultaneously measure multiple specific analytes within a single complex sample, a technique known as multiplex immunoassay. We have invented a new, simple technology that conducts standard enzyme-linked immunoassay assays within a plastic film device, allowing rapid and simultaneous quantitative detection of 10 or more analytes in multiple samples. The new technology interfaces with current liquid handling laboratory equipment (multichannel pipettes) and a colorimetric signal is detected with low-cost optical devices, such as a consumer flatbed scanner. The device is manufactured using a patented costefficient process and allows faster and easier multiplexed detection than standard assays whilst presenting similar sensitivities as demonstrated by proof-of-concept experiments. The new technology is being further explored as the basis for a portable multiplex immunoassay toolkit for a broad array of applications from lowcost point-of-care healthcare to biosecurity. doi:10.1016/j.jbiotec.2010.09.011 [P-C.46] BIOLIP, a biotechnology-oriented database of oil content in plants, algae, fungi and cyanobacteria A. Papini 1,∗ , S. Mosti 1 , P. Lio’ 2 , S. Haider 2 1
University of Florence, Italy University of Cambridge, United Kingdom Keywords: Fatty acids; Algae; Cyanobacteria; Lipid database 2
Lipids are an essential category of organic substances of interest in industrial fields, as biofuels (as alternatives to fossil fuels), biomasses for biotechnological uses and as health-related compounds. The main lipid sources are angiosperms species as Brassicaceae, soy, maize, oil palm and Jatropha. New crops are studied in order to obtain new varieties for with better yield, water and environmental necessities. Recently eukaryotic algae and cyanobacteria (Schenk et al., 2008) have been investigated to obtain lipids sources to increase productivity and to reduce the conflict with food cultivations. Our database BIOLIP (www.lipidresource.eu/biolip) aims to collect data on lipid content of organisms, with a biotechnology-