Multiple Mechanisms of the Synthesized Antimicrobial Peptide TS against Gram-Negative Bacteria for High Efficacy Antibacterial Action In Vivo

Zhang, Rui; Fan, Xuetong; Jiang, Xinglu; Zou, Mingyuan; Xiao, Han; Wu, Guoqiu

doi:10.3390/molecules26010060

Cited by 11 publications

(6 citation statements)

References 40 publications

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“…The antibacterial activities of lactoferricins are pH dependent and are reduced by various ions, such as Ca 2+ , Mg 2+ , Na + , and K + , with a similar trend also reported for lactoferrins [ 61 , 100 ]. This phenomenon has also been observed for other antimicrobial peptides, including bactenecins [ 128 ], polymyxin B [ 129 ], and the synthetic peptide TS [ 130 ]. The antibacterial activities of human lactoferrin and lactoferricin can be reduced not only by cations but also by anions, such as HEPES, PIPES, phosphate, citrate, and succinate [ 72 , 131 ].…”

Section: Antibacterial Activities Of Lactoferrins and Lactoferrin-derived Peptidesmentioning

confidence: 52%

Diverse Mechanisms of Antimicrobial Activities of Lactoferrins, Lactoferricins, and Other Lactoferrin-Derived Peptides

Gruden

Ulrih

2021

IJMS

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Lactoferrins are an iron-binding glycoprotein that have important protective roles in the mammalian body through their numerous functions, which include antimicrobial, antitumor, anti-inflammatory, immunomodulatory, and antioxidant activities. Among these, their antimicrobial activity has been the most studied, although the mechanism behind antimicrobial activities remains to be elucidated. Thirty years ago, the first lactoferrin-derived peptide was isolated and showed higher antimicrobial activity than the native lactoferrin lactoferricin. Since then, numerous studies have investigated the antimicrobial potencies of lactoferrins, lactoferricins, and other lactoferrin-derived peptides to better understand their antimicrobial activities at the molecular level. This review defines the current antibacterial, antiviral, antifungal, and antiparasitic activities of lactoferrins, lactoferricins, and lactoferrin-derived peptides. The primary focus is on their different mechanisms of activity against bacteria, viruses, fungi, and parasites. The role of their structure, amino-acid composition, conformation, charge, hydrophobicity, and other factors that affect their mechanisms of antimicrobial activity are also reviewed.

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Section: Antibacterial Activities Of Lactoferrins and Lactoferrin-derived Peptidesmentioning

confidence: 52%

Diverse Mechanisms of Antimicrobial Activities of Lactoferrins, Lactoferricins, and Other Lactoferrin-Derived Peptides

Gruden

Ulrih

2021

IJMS

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“…These bacteria significantly reduced the efficacy of antibiotics, whereas developing new therapeutic drugs has become an urgent priority ( de Kraker et al., 2016 ; Morrison and Zembower, 2020 ). AMPs as antibiotic preparations is an innovative approach have been used in the treatment of drug-resistant bacteria ( Zhang et al., 2020 ).…”

Section: Discussionmentioning

confidence: 99%

The antibacterial activity and mechanism of a novel peptide MR-22 against multidrug-resistant Escherichia coli

Tian,

Zhao,

Yang

et al. 2024

Front. Cell. Infect. Microbiol.

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IntroductionBacterial infections have become serious threats to human health, and the excessive use of antibiotics has led to the emergence of multidrug-resistant (MDR) bacteria. E. coli is a human bacterial pathogen, which can cause severe infectious. Antimicrobial peptides are considered the most promising alternative to traditional antibiotics.Materials and methodsThe minimum inhibitory concentration (MIC), minimum bactericidal concentration (MBC) and hemolytic activity were determined by the microdilution method. The antimicrobial kinetics of MR-22 against E. coli were studied by growth curves and time-killing curves. The cytotoxicity of MR-22 was detected by the CCK-8 assay. The antimicrobial activity of MR-22 in salt, serum, heat and trypsin was determined by the microdilution method. The antimicrobial mechanism of MR-22 against drug-resistant E. coli was studied by Scanning Electron Microscope, laser confocal microscopy, and Flow Cytometry. The in vivo antibacterial activity of MR-22 was evaluated by the mice model of peritonitis.Results and discussionIn this study, MR-22 is a new antimicrobial peptide with good activity that has demonstrated against MDR E. coli. The antimicrobial activity of MR-22 exhibited stability under conditions of high temperature, 10% FBS, and Ca2+. However, a decline of the activity was observed in the presence of Na+, serum, and trypsin. MR-22 had no significant cytotoxicity or hemolysis in vitro. SEM and fluorescent images revealed that MR-22 could disrupt the integrity of cell membrane. DCFH-DA indicated that MR-22 increased the content of reactive oxygen species, while it decreased the content of intracellular ATP. In mice model of peritonitis, MR-22 exhibited potent antibacterial activity in vivo. These results indicated that MR-22 is a potential drug candidate against drug-resistant E. coli.

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“…Te antimicrobial protein separated from botany such as corn peptide and soybean peptide could inhibit the activity of pathogens including bacteria, fungus, and viruses [11,12]. Te mechanism of antimicrobial protein on bacteria is multiple due to the diversity of sources [13].…”

Section: Introductionmentioning

confidence: 99%

Structural Analysis and Antimicrobial Mechanism of a Protein GBSPI-A from Ginkgo Biloba Seed

et al. 2023

Journal of Food Biochemistry

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Ginkgo biloba seed has antimicrobial activity. In this study, ginkgo biloba seed protein was prepared, identified, and named GBSPI-A, finding its construction was similar to 11-S globulin. Then, the influence of GBSPI-A on the cell membrane and physiological metabolism of K. pneumoniae and S. aureus were investigated. The results showed that GBSPI-A (20 mg/mL) destroyed the cell membrane, causing leakage of intracellular material and inhibited bacterial growth with an inhibition rate of approximately 80%. In addition, the GBSPI-A (10 mg/mL) caused the decreasing activity of ATPase and respiratory rate, and the respiratory depression rate was 7.24%. Furthermore, the decreasing ATP synthesis and intracellular β-galactosidase activity led to an insufficient supply of physiological metabolic energy. Therefore, the results showed that GBSPI-A could be used as a natural bacteriostatic agent to replace related drugs and also provide a new insight into the application of GBSPI-A in food safety.

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Multiple Mechanisms of the Synthesized Antimicrobial Peptide TS against Gram-Negative Bacteria for High Efficacy Antibacterial Action In Vivo

Cited by 11 publications

References 40 publications

Diverse Mechanisms of Antimicrobial Activities of Lactoferrins, Lactoferricins, and Other Lactoferrin-Derived Peptides

Diverse Mechanisms of Antimicrobial Activities of Lactoferrins, Lactoferricins, and Other Lactoferrin-Derived Peptides

The antibacterial activity and mechanism of a novel peptide MR-22 against multidrug-resistant Escherichia coli

Structural Analysis and Antimicrobial Mechanism of a Protein GBSPI-A from Ginkgo Biloba Seed

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