ArticleThe Biochemical journal1998
Identification and characterization of the antimicrobial peptide corresponding to C-terminal beta-sheet domain of tenecin 1, an antibacterial protein of larvae of Tenebrio molitor.
Article in The Biochemical journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 58 citations in OpenAlex.
- Efficient in planta production of amidated antimicrobial peptides that are active against drug-resistant ESKAPE pathogens.Nature communications · 2023Article
- A Novel β-Hairpin Peptide Z-d14CFR Enhances Multidrug-Resistant Bacterial Clearance in a Murine Model of Mastitis.International journal of molecular sciences · 2022Article
- Biosurfactants Induce Antimicrobial Peptide Production through the Activation ofInternational journal of molecular sciences · 2020Article
- Two Roles for theInsects · 2020Article
- BIOPEP-UWM Database of Bioactive Peptides: Current Opportunities.International journal of molecular sciences · 2019Article
- Establishing a reference array for the CS-αβ superfamily of defensive peptides.BMC research notes · 2016Article
- Trans-generational Immune Priming Protects the Eggs Only against Gram-Positive Bacteria in the Mealworm Beetle.PLoS pathogens · 2015Article
- Transcriptome profiling of the intoxication response of Tenebrio molitor larvae to Bacillus thuringiensis Cry3Aa protoxin.PloS one · 2012Article
- Limiting an antimicrobial peptide to the lipid-water interface enhances its bacterial membrane selectivity: a case study of MSI-367.Biochemistry · 2010Article
- Anticandida activity is retained in P-113, a 12-amino-acid fragment of histatin 5.Antimicrobial agents and chemotherapy · 2001Article
- Identification and characterization of novel antimicrobial decapeptides generated by combinatorial chemistry.Antimicrobial agents and chemotherapy · 1998Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
An active fragment was identified from tenecin 1, an antibacterial protein belonging to the insect defensin family, by synthesizing the peptides corresponding to the three regions of tenecin 1. Only the fragment corresponding to the C-terminal beta-sheet domain showed activity against fungi as well as Gram-positive and Gram-negative bacteria, whereas tenecin 1, the native protein, showed activity only against Gram-positive bacteria. CD spectra indicated that each fragment in a membrane-mimetic environment might adopt a secondary structure corresponding to its region in the protein. The leakage of dye from liposomes induced by this fragment suggested that this fragment acts on the membrane of pathogens as a primary mode of action. A comparison between the structure and the activity of each fragment indicated that a net positive charge was a prerequisite factor for activity. To the best of our knowledge this is the first report in which the fragment corresponding to the beta-sheet region in antibacterial proteins, which consists of alpha-helical and beta-sheet regions, has been identified as a primary active fragment.
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