Antimicrobial peptides properties beyond growth inhibition and bacterial killing

Castillo‐Juárez, Israel; Blancas-Luciano, Blanca Esther; García‐Contreras, Rodolfo; Fernández-Presas, Ana María

doi:10.7717/peerj.12667

Cited by 17 publications

(12 citation statements)

References 125 publications

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“…Generally, AMPs have a net positive charge (+2 to +11), allowing an electrostatic interaction with negatively charged phospholipids in the bacterial membranes. They are amphipathic molecules, which make them soluble and incorporate into the lipid bilayer of the cell membrane, leading to membrane perforation, cell lysis, and death ( Castillo-Juárez et al, 2022 ).…”

Section: Discussionmentioning

confidence: 99%

Anti-methicillin-resistant Staphylococcus aureus and antibiofilm activity of new peptides produced by a Brevibacillus strain

Ogunsile,

Songnaka,

Sawatdee

et al. 2023

PeerJ

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Background Methicillin-resistant Staphylococcus aureus (MRSA) is listed as a highly prioritized pathogen by the World Health Organization (WHO) to search for effective antimicrobial agents. Previously, we isolated a soil Brevibacillus sp. strain SPR19 from a botanical garden, which showed anti-MRSA activity. However, the active substances were still unknown. Methods The cell-free supernatant of this bacterium was subjected to salt precipitation, cation exchange, and reversed-phase chromatography. The antimicrobial activity of pure substances was determined by broth microdilution assay. The peptide sequences and secondary structures were characterized by tandem mass spectroscopy and circular dichroism (CD), respectively. The most active anti-MRSA peptide underwent a stability study, and its mechanism was determined through scanning electron microscopy, cell permeability assay, time-killing kinetics, and biofilm inhibition and eradication. Hemolysis was used to evaluate the peptide toxicity. Results The pure substances (BrSPR19-P1 to BrSPR19-P5) were identified as new peptides. Their minimum inhibition concentration (MIC) and minimum bactericidal concentration (MBC) against S. aureus and MRSA isolates ranged from 2.00 to 32.00 and 2.00 to 64.00 µg/mL, respectively. The sequence analysis of anti-MRSA peptides revealed a length ranging from 12 to 16 residues accompanied by an amphipathic structure. The physicochemical properties of peptides were predicted such as pI (4.25 to 10.18), net charge at pH 7.4 (−3 to +4), and hydrophobicity (0.12 to 0.96). The CD spectra revealed that all peptides in the water mainly contained random coil structures. The increased proportion of α-helix structure was observed in P2−P5 when incubated with SDS. P2 (NH2-MFLVVKVLKYVV-COOH) showed the highest antimicrobial activity and high stability under stressed conditions such as temperatures up to 100 °C, solution of pH 3 to 10, and proteolytic enzymes. P2 disrupted the cell membrane and caused bacteriolysis, in which its action was dependent on the incubation time and peptide concentration. Antibiofilm activity of P2 was determined by which the half-maximal inhibition of biofilm formation was observed at 2.92 and 4.84 µg/mL for S. aureus TISTR 517 and MRSA isolate 2468, respectively. Biofilm eradication of tested pathogens was found at the P2 concentration of 128 µg/mL. Furthermore, P2 hemolytic activity was less than 10% at concentrations up to 64 µg/mL, which reflected the hemolysis index thresholds of 32. Conclusion Five novel anti-MRSA peptides were identified from SPR19. P2 was the most active peptide and was demonstrated to cause membrane disruption and cell lysis. The P2 activity was dependent on the peptide concentration and exposure time. This peptide had antibiofilm activity against tested pathogens and was compatible with human erythrocytes, supporting its potential use as an anti-MRSA agent in this post-antibiotic era.

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Section: Discussionmentioning

confidence: 99%

Anti-methicillin-resistant Staphylococcus aureus and antibiofilm activity of new peptides produced by a Brevibacillus strain

Ogunsile,

Songnaka,

Sawatdee

et al. 2023

PeerJ

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“…The cationic amphipathic structure of these AMPs allows them to interact with negatively charged bacterial membranes, causing membrane lysis or invasion to carry out non-membranolytic mechanisms ( Di Somma et al., 2020 ). AMPs exhibit additional antimicrobial activity as a result of non-membranolytic mechanisms, which are particularly useful in disruption genes or proteins that are essential for biofilm formation, function, and virulence ( Luo and Song, 2021 ; Castillo-Juárez et al., 2022 ). There has been recent interest in isolating particular AMPs from plant essential oils.…”

Section: Novel Strategies For Eradicationmentioning

confidence: 99%

Strategies for combating antibiotic resistance in bacterial biofilms

Grooters,

Ku,

Richter

et al. 2024

Front. Cell. Infect. Microbiol.

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Biofilms, which are complexes of microorganisms that adhere to surfaces and secrete protective extracellular matrices, wield substantial influence across diverse domains such as medicine, industry, and environmental science. Despite ongoing challenges posed by biofilms in clinical medicine, research in this field remains dynamic and indeterminate. This article provides a contemporary assessment of biofilms and their treatment, with a focus on recent advances, to chronicle the evolving landscape of biofilm research.

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“…Bioactive antimicrobial peptides also exhibit antivirulence property activity against foodborne pathogens at subinhibitory concentrations. Various BAPs have bactericidal effects on biofilm formation and can eradicate infections in animal models [ 143 ].…”

Section: Antimicrobial Applications Of Baps Against Foodborne Pathogensmentioning

confidence: 99%

Microbial‐ and Plant‐Derived Bioactive Peptides and Their Applications against Foodborne Pathogens: Current Status and Future Prospects

Parvez,

Jubyda,

Ayaz

et al. 2024

International Journal of Microbiology

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Bioactive peptides (BAPs) obtained from plants and microbes have been thoroughly explored and studied due to their prophylactic properties. The use of BAPs seems to be a promising substitute for several currently available antibiotics because of their antimicrobial properties against foodborne pathogens. BAPs have several other useful properties including antitumor, antihypertensive, antioxidant, antiobesity, and antidiabetic activities. Nowadays, scientists have attempted to recombinantly synthesize bioactive peptides to study their characteristics and potential uses, since BAPs are not found in large quantities in nature. Many pathogenic microorganisms including foodborne pathogens are becoming resistant to various antibiotics. To combat these pathogens, scientists are working to find novel, innovative, and safe antimicrobial agents. Plant- and microbe-based BAPs have demonstrated noteworthy antimicrobial activity against a wide range of pathogenic microorganisms, including foodborne pathogens. BAPs can kill pathogenic microorganisms by disrupting membrane integrity, inhibiting DNA and RNA synthesis, preventing protein synthesis, blocking protein activity, or interacting with certain intracellular targets. In addition, the positive effect of BAP consumption extends to gut microbiota modulation and affects the equilibrium of reactive oxygen species in the gut. This article discusses recombinant BAPs, BAPs generated from plants and microbes, and their antimicrobial applications and modes of action for controlling foodborne pathogens.

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Antimicrobial peptides properties beyond growth inhibition and bacterial killing

Cited by 17 publications

References 125 publications

Anti-methicillin-resistant Staphylococcus aureus and antibiofilm activity of new peptides produced by a Brevibacillus strain

Anti-methicillin-resistant Staphylococcus aureus and antibiofilm activity of new peptides produced by a Brevibacillus strain

Strategies for combating antibiotic resistance in bacterial biofilms

Microbial‐ and Plant‐Derived Bioactive Peptides and Their Applications against Foodborne Pathogens: Current Status and Future Prospects

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