Design, expression, and characterization of the hybrid antimicrobial peptide T-catesbeianin-1 based on FyuA

2018 ◽  
Vol 24 (1) ◽  
pp. e3059 ◽  
Author(s):  
Huihui Xu ◽  
Kunyuan Tie ◽  
Yang Zhang ◽  
Xin Feng ◽  
Yuan Cao ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Peptide T

scholarly journals Development and characterization of phosphatidylcholine nanovesicles containing the antimicrobial peptide nisin

2010 ◽  
Vol 43 (4) ◽  
pp. 1198-1203 ◽  
Author(s):  
Patrícia da Silva Malheiros ◽  
Yasmine Miguel Serafini Micheletto ◽  
Nádya Pesce da Silveira ◽  
Adriano Brandelli
Keyword(s):  
Antimicrobial Peptide

Synthesis and characterization of indolicidin, a tryptophan-rich antimicrobial peptide from bovine neutrophils *

2009 ◽  
Vol 45 (5) ◽  
pp. 401-409 ◽  
Author(s):  
ROBERT J. VAN ABEL ◽  
YI-QUAN TANG ◽  
V.S.V. RAO ◽  
CRAIG H. DOBBS ◽  
DAT TRAN ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Synthesis And Characterization ◽  
Bovine Neutrophils

Characterization of virus/double-stranded RNA-dependent induction of antimicrobial peptide hepcidin in trout macrophages

2007 ◽  
Vol 31 (12) ◽  
pp. 1297-1309 ◽  
Author(s):  
Pinwen Peter Chiou ◽  
Chun-Mean Lin ◽  
Niels C. Bols ◽  
Thomas T. Chen
Keyword(s):  
Antimicrobial Peptide ◽  
Double Stranded Rna

scholarly journals Purification and characterization of three isoforms of chrysophsin, a novel antimicrobial peptide in the gills of the red sea bream, Chrysophrys major

2003 ◽  
Vol 270 (4) ◽  
pp. 675-686 ◽  
Author(s):  
Noriaki Iijima ◽  
Norio Tanimoto ◽  
Yohko Emoto ◽  
Yohko Morita ◽  
Kazumasa Uematsu ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Red Sea ◽  
Sea Bream ◽  
Red Sea Bream ◽  
Purification And Characterization

scholarly journals In vitro and In Silico Approach For Characterization of Antimicrobial Peptide From Probiotics Against Staphylococcus Aureus and Escherichia Coli

2021 ◽  
Author(s):  
Amrutha Bindu ◽  
Lakshmi Devi
Keyword(s):  
Amino Acid ◽  
Antimicrobial Peptide ◽  
Lactobacillus Plantarum ◽  
Exchange Chromatography ◽  
Amino Acid Sequences ◽  
Proteinase K ◽  
Kinetic Assay ◽  
Wide Range

Abstract The focus of present study was to characterize antimicrobial peptide produced by probiotic cultures, Enterococcus durans DB-1aa (MCC4243), Lactobacillus plantarum Cu2-PM7 (MCC4246) and Lactobacillus fermentum Cu3-PM8 (MCC4233) against Staphylococus aureus and E. coli. The growth kinetic assay revealed 24 h of incubation to be optimum for bacteriocin production. The partially purified compound after ion-exchange chromatography was found to be thermoresistant and stable under wide range of pH. The compound was sensitive to proteinase-K, but resistant to trypsin, a-amylase and lipase. The apparent molecular weight of bacteriocin from MCC4243 and MCC4246 was found to be 3.5 KDa. Translated partial amino acid sequence of plnA gene in MCC4246 displayed 48 amino acid sequences showing 100% similarity with plantaricin A of Lactobacillus plantarum (WP_0036419). The sequence revealed 7 β sheets, 6 α sheets, 6 predicted coils and 9 predicted turns. The functions on cytoplasm show 10.82 isoelectric point and 48.6% hydrophobicity. The molecular approach of using Geneious Prime software and protein prediction data base for characterization of bacteriocin is novel and predicts “KSSAYSLQMGATAIKQVKKLFKKWGW” as peptide responsible for antimicrobial activity. The study provides information about broad spectrum bacteriocin in native probiotic culture and paves a way towards its application in functional foods as biopreservative agents.

scholarly journals Functional Characterization of a Novel Promoter Element Required for an Innate Immune Response in Drosophila

2003 ◽  
Vol 23 (22) ◽  
pp. 8272-8281 ◽  
Author(s):  
Hanna Uvell ◽  
Ylva Engström
Keyword(s):  
Gene Expression ◽  
Antimicrobial Peptide ◽  
Functional Characterization ◽  
Binding Activity ◽  
Innate Immune ◽  
Site Directed Mutagenesis ◽  
Promoter Element ◽  
Peptide Gene ◽  
Inducible Genes

ABSTRACT Innate immune reactions are crucial processes of metazoans to protect the organism against overgrowth of faster replicating microorganisms. Drosophila melanogaster is a precious model for genetic and molecular studies of the innate immune system. In response to infection, the concerted action of a battery of antimicrobial peptides ensures efficient killing of the microbes. The induced gene expression relies on translocation of the Drosophila Rel transcription factors Relish, Dif, and Dorsal to the nucleus where they bind to κB-like motifs in the promoters of the inducible genes. We have identified another putative promoter element, called region 1 (R1), in a number of antimicrobial peptide genes. Site-directed mutagenesis of the R1 site diminished Cecropin A1 (CecA1) expression in transgenic Drosophila larvae and flies. Infection of flies induced a nuclear R1-binding activity that was unrelated to the κB-binding activity in the same extracts. Although the R1 motif was required for Rel protein-mediated CecA1 expression in cotransfection experiments, our data argue against it being a direct target for the Drosophila Rel proteins. We propose that the R1 and κB motifs are targets for distinct regulatory complexes that act in concert to promote high levels of antimicrobial peptide gene expression in response to infection.

scholarly journals Characterization of a novel antimicrobial peptide from buffalo casein hydrolysate based on live bacteria adsorption

2020 ◽  
Vol 103 (12) ◽  
pp. 11116-11128
Author(s):  
Qiong Zhao ◽  
Yanan Shi ◽  
Xuefeng Wang ◽  
Aixiang Huang
Keyword(s):  
Antimicrobial Peptide ◽  
Casein Hydrolysate ◽  
Live Bacteria
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