ArticleMarine drugs2016
Structure and Bioactivity of a Modified Peptide Derived from the LPS-Binding Domain of an Anti-Lipopolysaccharide Factor (ALF) of Shrimp.
Article in Marine drugs, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Recombinant Expression and Antimicrobial Mechanism of Cysteine-Rich Antimicrobial Peptides fromMarine drugs · 2026Article
- Heterologous Expression and Antimicrobial Targets of a Novel Glycine-Rich Antimicrobial Peptide fromMarine drugs · 2025Article
- Heterologous Expression and Antimicrobial Mechanism of a Cysteine-Rich Peptide from BarnacleMicroorganisms · 2025Article
- Machine learning and genetic algorithm-guided directed evolution for the development of antimicrobial peptides.Journal of advanced research · 2025Article
- Peptide Dimerization as a Strategy for the Development of Antileishmanial Compounds.Molecules (Basel, Switzerland) · 2024Article
- Antimicrobial Spectrum of Activity and Mechanism of Action of Linear Alpha-Helical Peptides Inspired by Shrimp Anti-Lipopolysaccharide Factors.Biomolecules · 2023Article
- The Antioxidant Effect of Natural Antimicrobials in Shrimp Primary Intestinal Cells Infected withAntioxidants (Basel, Switzerland) · 2022Article
- Discovery and Characterization of a New Crustin Antimicrobial Peptide fromPharmaceutics · 2022Article
- Article
- A Lymphoid Organ Specific Anti-Lipopolysaccharide Factor fromMarine drugs · 2021Article
- Article
- Characterization of a Lymphoid Organ Specific Anti-lipopolysaccharide Factor From Shrimp Reveals Structure-Activity Relationship of the LPS-Binding Domain.Frontiers in immunology · 2019Article
- Identification and characterization of a novel goose-type and chicken-type lysozyme genes in Chinese rare minnow (Gobiocypris rarus) with potent antimicrobial activity.Genes & genomics · 2018Article
- Multiple Isoforms of Anti-Lipopolysaccharide Factors and Their Antimicrobial Functions in the Ridgetail PrawnMarine drugs · 2018Article
- Antiviral Activity of Ctn[15-34], A Cathelicidin-Derived Eicosapeptide, Against Infectious Myonecrosis Virus in Litopenaeus vannamei Primary Hemocyte Cultures.Food and environmental virology · 2017Article
- Recombinant Expression of a Modified Shrimp Anti-Lipopolysaccharide Factor Gene in Pichia pastoris GS115 and Its Characteristic Analysis.Marine drugs · 2016Article
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The lipopolysaccharide binding domain (LBD) in anti-lipopolysaccharide factor (ALF) is the main functional element of ALF, which exhibits antimicrobial activities. Our previous studies show that the peptide LBDv, synthesized based on the modified sequence of LBD (named LBD2) from FcALF2, exhibited an apparently enhanced antimicrobial activity. To learn the prospect of LBDv application, the characteristics of LBDv were analyzed in the present study. The LBDv peptide showed higher antimicrobial and bactericidal activities compared with LBD2. These activities of the LBDv peptide were stable after heat treatment. LBDv could also exhibit in vivo antimicrobial activity to Vibrio harveyi. The LBDv peptide was found to bind bacteria, quickly cause bacterial agglutination, and kill bacteria by damaging their membrane integrity. Structure analysis showed that both LBDv and LBD2 held the β-sheet structure, and the positive net charge and amphipathicity characteristic were speculated as two important components for their antimicrobial activity. The cytotoxicity of LBDv was evaluated in cultured Spodoptera frugiperda (Sf9) cells and Cherax quadricarinatus hemocytes. More than 80% cells could survive with the LBDv concentration up to 16 μM. Collectively, these findings highlighted the potential antimicrobial mechanism of LBD peptides, and provided important information for the commercial use of LBDv in the future.
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