Optimized Expression and Characterization of Antimicrobial Peptides, LPcin Analogs

2015 ◽  
Vol 36 (4) ◽  
pp. 1148-1154 ◽  
Author(s):  
Ji-Sun Kim ◽  
Ji-Ho Jeong ◽  
Kyung-Sup Kim ◽  
Yongae Kim
Keyword(s):  
Antimicrobial Peptides

scholarly journals Isolation and characterization of a novel class of plant antimicrobial peptides form Mirabilis jalapa L. seeds.

1992 ◽  
Vol 267 (4) ◽  
pp. 2228-2233 ◽  
Author(s):  
B P Cammue ◽  
M F De Bolle ◽  
F R Terras ◽  
P Proost ◽  
J Van Damme ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Isolation And Characterization ◽  
Mirabilis Jalapa

Cloning and characterization of two cDNA clones encoding seed-specific antimicrobial peptides from Mirabilis jalapa L.

1995 ◽  
Vol 28 (4) ◽  
pp. 713-721 ◽  
Author(s):  
Miguel F. C. De Bolle ◽  
Kristel Eggermont ◽  
Rachael E. Duncan ◽  
Rupert W. Osborn ◽  
Franky R. G. Terras ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Cdna Clones ◽  
Mirabilis Jalapa

Design and characterization of novel hybrid antimicrobial peptides based on cecropin A, LL-37 and magainin II

Peptides ◽  
2012 ◽  
Vol 33 (2) ◽  
pp. 197-205 ◽  
Author(s):  
Marc A. Fox ◽  
Joanne E. Thwaite ◽  
David O. Ulaeto ◽  
Timothy P. Atkins ◽  
Helen S. Atkins
Keyword(s):  
Antimicrobial Peptides ◽  
Cecropin A ◽  
Magainin Ii

Characterization of novel antimicrobial peptides from the skin of the endangered frog Odorrana ishikawae by shotgun cDNA cloning

2011 ◽  
Vol 412 (4) ◽  
pp. 673-677 ◽  
Author(s):  
Eiko Iwakoshi-Ukena ◽  
Miyuki Soga ◽  
Genya Okada ◽  
Tamotsu Fujii ◽  
Masayuki Sumida ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Cdna Cloning

scholarly journals Blood Compatibility—An Important but Often Forgotten Aspect of the Characterization of Antimicrobial Peptides for Clinical Application

2019 ◽  
Vol 20 (21) ◽  
pp. 5426
Author(s):  
Stephan Harm ◽  
Karl Lohner ◽  
Ute Fichtinger ◽  
Claudia Schildböck ◽  
Jennifer Zottl ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Chain Length ◽  
Blood Compatibility ◽  
Acyl Chain ◽  
Antimicrobial Properties ◽  
Polymyxin B ◽  
Acyl Chain Length ◽  
Human Blood Cells ◽  
Plasmatic Coagulation

Acylation of antimicrobial peptides mimics the structure of the natural lipopeptide polymyxin B, and increases antimicrobial and endotoxin-neutralizing activities. In this study, the antimicrobial properties of lactoferrin-based LF11 peptides as well as blood compatibility as a function of acyl chain length were investigated. Beyond the classical hemolysis test, the biocompatibility was determined with human leukocytes and platelets, and the influence of antimicrobial peptides (AMPs) on the plasmatic coagulation and the complement system was investigated. The results of this study show that the acylation of cationic peptides significantly reduces blood tolerance. With increasing acyl chain length, the cytotoxicity of LF11 peptides to human blood cells also increased. This study also shows that acylated cationic antimicrobial peptides are inactivated by the presence of heparin. In addition, it could be shown that the immobilization of LF11 peptides leads to a loss of their antimicrobial properties.

scholarly journals Insect Gut Symbiont Susceptibility to Host Antimicrobial Peptides Caused by Alteration of the Bacterial Cell Envelope

2015 ◽  
Vol 290 (34) ◽  
pp. 21042-21053 ◽  
Author(s):  
Jiyeun Kate Kim ◽  
Dae Woo Son ◽  
Chan-Hee Kim ◽  
Jae Hyun Cho ◽  
Roberta Marchetti ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Bacterial Cell ◽  
Biochemical Characterization ◽  
Cultured Cells ◽  
Cell Envelope ◽  
Bacterial Cell Envelope ◽  
Symbiotic Interactions ◽  
Gut Symbionts ◽  
Insect Gut

The molecular characterization of symbionts is pivotal for understanding the cross-talk between symbionts and hosts. In addition to valuable knowledge obtained from symbiont genomic studies, the biochemical characterization of symbionts is important to fully understand symbiotic interactions. The bean bug (Riptortus pedestris) has been recognized as a useful experimental insect gut symbiosis model system because of its cultivatable Burkholderia symbionts. This system is greatly advantageous because it allows the acquisition of a large quantity of homogeneous symbionts from the host midgut. Using these naïve gut symbionts, it is possible to directly compare in vivo symbiotic cells with in vitro cultured cells using biochemical approaches. With the goal of understanding molecular changes that occur in Burkholderia cells as they adapt to the Riptortus gut environment, we first elucidated that symbiotic Burkholderia cells are highly susceptible to purified Riptortus antimicrobial peptides. In search of the mechanisms of the increased immunosusceptibility of symbionts, we found striking differences in cell envelope structures between cultured and symbiotic Burkholderia cells. The bacterial lipopolysaccharide O antigen was absent from symbiotic cells examined by gel electrophoretic and mass spectrometric analyses, and their membranes were more sensitive to detergent lysis. These changes in the cell envelope were responsible for the increased susceptibility of the Burkholderia symbionts to host innate immunity. Our results suggest that the symbiotic interactions between the Riptortus host and Burkholderia gut symbionts induce bacterial cell envelope changes to achieve successful gut symbiosis.

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