Matches in SemOpenAlex for { <https://semopenalex.org/work/W4353030714> ?p ?o ?g. }
Showing items 1 to 64 of
64
with 100 items per page.
- W4353030714 abstract "Optimizing synthetic antimicrobial peptides for safe and enhanced activity against fungal and bacterial pathogens is useful for genetic engineering of plants for resistance to plant pathogens and their associated mycotoxins. Nine synthetic peptides modeled after lytic peptides tachyplesin 1, D4E1 from cecropin A and protegrin 1 were added to germinated spores of fungal species Aspergillus flavus, Rhizopus stolonifer, Fusarium oxysporum f. sp. vasinfectum, F. verticillioides, F. graminearum, Claviceps purpurea, Verticillium dahliae, Thielaviopsis basicola and bacterial cultures of Psuedomonas syringae p.v. tabaci and Xanthomonas campestris p.v. campestris at different doses and inhibitory dose response curves were modeled to assess antimicrobial activity. Peptides GV185 and GV187, modified from tachyplesin 1, had superior abilities to inhibit fungal and bacterial growth (50% inhibitory concentrations or IC50 ranging from 0.1 to 8.7 µM). Rhizopus stolonifer (IC50 = 8.1 µM), A. flavus (IC50 = 3.1 µM) and F. graminearum (IC50 = 2.2 µM) were less inhibited by GV185 and GV187 than all the remaining fungi (IC50 = 1.4 µM) and bacteria (IC50 = 0.1 µM). Of the remaining peptides, GV193, GV195 and GV196 (IC50 range 0.9 to 6.6 µM) inhibited fungal growth of A. flavus, F. verticillioides and F. graminearum less than GV185 and GV187 (IC50 range 0.8 to 3.9 µM), followed by GV197 (IC50 range 0.8 - 9.1 µM) whereas GV190 and GV192 inhibited poorly (IC50 range 28.2 to 36.6 µM and 15.5 to 19.4 µM, respectively) and GV198 stimulated growth. GV185 and GV187 had slightly weaker hydrophobic and cationic residues than other tachyplesin 1 modified peptides, but still had unexpectedly high lytic activity. Germinated fungal spores of R. stolonifer and F. graminearum exposed to these two peptides and D4E1 and AGM182 appeared wrinkled with perforations near potential cytoplasmic leakage, which provided evidence of plasma membrane and cell wall lysis. We conclude that peptides GV185 and GV187 are promising candidates for genetic engineering of crops for resistance to plant pathogenic bacteria and fungi including A. flavus and aflatoxin contamination." @default.
- W4353030714 created "2023-03-23" @default.
- W4353030714 creator A5011860847 @default.
- W4353030714 creator A5037013779 @default.
- W4353030714 creator A5038518802 @default.
- W4353030714 creator A5050044578 @default.
- W4353030714 date "2023-03-22" @default.
- W4353030714 modified "2023-09-27" @default.
- W4353030714 title "Broad-spectrum antimicrobial activity of synthetic peptides GV185 and GV187" @default.
- W4353030714 doi "https://doi.org/10.1094/pdis-11-22-2572-re" @default.
- W4353030714 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36947838" @default.
- W4353030714 hasPublicationYear "2023" @default.
- W4353030714 type Work @default.
- W4353030714 citedByCount "0" @default.
- W4353030714 crossrefType "journal-article" @default.
- W4353030714 hasAuthorship W4353030714A5011860847 @default.
- W4353030714 hasAuthorship W4353030714A5037013779 @default.
- W4353030714 hasAuthorship W4353030714A5038518802 @default.
- W4353030714 hasAuthorship W4353030714A5050044578 @default.
- W4353030714 hasConcept C100544194 @default.
- W4353030714 hasConcept C202751555 @default.
- W4353030714 hasConcept C2777292910 @default.
- W4353030714 hasConcept C2777752497 @default.
- W4353030714 hasConcept C2778753027 @default.
- W4353030714 hasConcept C2778867309 @default.
- W4353030714 hasConcept C2779430813 @default.
- W4353030714 hasConcept C2781131586 @default.
- W4353030714 hasConcept C31903555 @default.
- W4353030714 hasConcept C4937899 @default.
- W4353030714 hasConcept C55493867 @default.
- W4353030714 hasConcept C59822182 @default.
- W4353030714 hasConcept C86803240 @default.
- W4353030714 hasConcept C89423630 @default.
- W4353030714 hasConceptScore W4353030714C100544194 @default.
- W4353030714 hasConceptScore W4353030714C202751555 @default.
- W4353030714 hasConceptScore W4353030714C2777292910 @default.
- W4353030714 hasConceptScore W4353030714C2777752497 @default.
- W4353030714 hasConceptScore W4353030714C2778753027 @default.
- W4353030714 hasConceptScore W4353030714C2778867309 @default.
- W4353030714 hasConceptScore W4353030714C2779430813 @default.
- W4353030714 hasConceptScore W4353030714C2781131586 @default.
- W4353030714 hasConceptScore W4353030714C31903555 @default.
- W4353030714 hasConceptScore W4353030714C4937899 @default.
- W4353030714 hasConceptScore W4353030714C55493867 @default.
- W4353030714 hasConceptScore W4353030714C59822182 @default.
- W4353030714 hasConceptScore W4353030714C86803240 @default.
- W4353030714 hasConceptScore W4353030714C89423630 @default.
- W4353030714 hasLocation W43530307141 @default.
- W4353030714 hasLocation W43530307142 @default.
- W4353030714 hasOpenAccess W4353030714 @default.
- W4353030714 hasPrimaryLocation W43530307141 @default.
- W4353030714 hasRelatedWork W1967109557 @default.
- W4353030714 hasRelatedWork W2135263222 @default.
- W4353030714 hasRelatedWork W2141198762 @default.
- W4353030714 hasRelatedWork W2286309970 @default.
- W4353030714 hasRelatedWork W2364659678 @default.
- W4353030714 hasRelatedWork W2366428059 @default.
- W4353030714 hasRelatedWork W3163236910 @default.
- W4353030714 hasRelatedWork W3212517262 @default.
- W4353030714 hasRelatedWork W4353030714 @default.
- W4353030714 hasRelatedWork W87592838 @default.
- W4353030714 isParatext "false" @default.
- W4353030714 isRetracted "false" @default.
- W4353030714 workType "article" @default.