Characterisation of cell membrane interaction mechanisms of antimicrobial peptides by electrical bilayer recording

Priyadarshini, Diana; Ivica, Josip; Separovic, Frances; Planque, Maurits R.R. de

doi:10.1016/j.bpc.2021.106721

Cited by 16 publications

(11 citation statements)

References 41 publications

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“…The urge to eradicate multidrug-resistant bacterial infections powered the use of AMPs as an attractive strategy with high structural diversity and broad-spectrum antimicrobial activity. − Rational design approaches have been used to generate synthetic analogs of antimicrobial peptides, reducing the limitations and increasing advantages. , However, several AMPs have failed in phase II and III testing because AMPs are vulnerable to proteolysis and have toxicity associated with mammalian membrane lysis . We have shown a new strategy that improved the antimicrobial peptide analogs.…”

Section: Discussionmentioning

confidence: 99%

Site-Specific Isopeptide Bond Formation: A Powerful Tool for the Generation of Potent and Nontoxic Antimicrobial Peptides

et al. 2022

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Antimicrobial peptides (AMPs) have the potential to treat multidrug-resistant bacterial infections. However, the clinical application of AMPs is prevented by their toxicity and poor proteolytic stability. Here, a site-specific approach is used to generate new AMPs to improve their efficacy against bacterial pathogens while reducing their toxicity. We modified and generated a new series of antimicrobial peptides from the leucine- and lysine-rich antimicrobial peptide Amp1L (LKLLKKLLKKLLKLL) by the site-specific incorporation of an isopeptide bond while retaining the peptide’s size, sequence, charge, and molecular weight. This single bond switch provides the peptides with a weak helical conformation, strong antimicrobial activity, resistance to proteolytic degradation, low toxicity, and lower hemolytic activity. This new site-specific approach offers a powerful tool for developing potent and nontoxic antimicrobial drugs.

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Section: Discussionmentioning

confidence: 99%

Site-Specific Isopeptide Bond Formation: A Powerful Tool for the Generation of Potent and Nontoxic Antimicrobial Peptides

et al. 2022

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“…AMPs are 12-50 amino acid long peptides that have been discovered in all forms of life, including bacteria, vertebrates, and invertebrate species [9,10,[13][14][15]. Based on their physicochemical properties, they likely have a direct activity on the membrane bilayer [16,17], although sometimes they also have an intracellular target. AMPs are generally cationic and amphipathic; their net positive charge enhances electrostatic interactions with anionic bacterial membranes, while the amphipathic structure leads to membrane insertion, destabilization and disruption.…”

Section: Of 18mentioning

confidence: 99%

WMR Peptide as Antifungal and Antibiofilm against Albicans and Non-Albicans Candida Species: Shreds of Evidence on the Mechanism of Action

Maione

Bellavita

Alteriis

et al. 2022

IJMS

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Candida species are the most common fungal pathogens infecting humans and can cause severe illnesses in immunocompromised individuals. The increased resistance of Candida to traditional antifungal drugs represents a great challenge in clinical settings. Therefore, novel approaches to overcome antifungal resistance are desired. Here, we investigated the use of an antimicrobial peptide WMR against Candida albicans and non-albicans Candida species in vitro and in vivo. Results showed a WMR antifungal activity on all Candida planktonic cells at concentrations between 25 μM to >50 μM and exhibited activity at sub-MIC concentrations to inhibit biofilm formation and eradicate mature biofilm. Furthermore, in vitro antifungal effects of WMR were confirmed in vivo as demonstrated by a prolonged survival rate of larvae infected by Candida species when the peptide was administered before or after infection. Additional experiments to unravel the antifungal mechanism were performed on C. albicans and C. parapsilosis. The time-killing curves showed their antifungal activity, which was further confirmed by the induced intracellular and mitochondrial reactive oxygen species accumulation; WMR significantly suppressed drug efflux, down-regulating the drug transporter encoding genes CDR1. Moreover, the ability of WMR to penetrate within the cells was demonstrated by confocal laser scanning microscopy. These findings provide novel insights for the antifungal mechanism of WMR against Candida albicans and non-albicans, providing fascinating scenarios for the identification of new potential antifungal targets.

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“…The urge to eradicate multidrug-resistant bacteria that contaminate food has driven the use of AMPs in food preservation as an alternative with greater safety and broad-spectrum antimicrobial activity . A bovine neutrophil-derived host defense peptide, IDR-1018, obtained by modification of bactenecin, was brought to our attention.…”

Section: Resultsmentioning

confidence: 99%

Design of a Novel Lysine Isopeptide 1018KI11 with Potent Antimicrobial Activity as a Safe and Stable Food Preservative Candidate

Wang,

Yang,

Dong

et al. 2024

J. Agric. Food Chem.

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Antimicrobial peptides are potent food additive candidates, but most of them are sensitive to proteases, which limits their application. Therefore, we substituted arginine for lysine and introduced a lysine isopeptide bond to peptide IDR-1018 in order to improve its enzymatic stability. Subsequently, the protease stability and antimicrobial/antibiofilm activity of the novel peptides (1018K2−1018KI11) were investigated. The data revealed that the antienzymatic potential of 1018KI11 to bromelain and papain increased by 2−8 folds and 16 folds, respectively. The minimum inhibitory concentration (MIC) of 1018KI11 against methicillinresistant Staphylococcus aureus (MRSA) ATCC43300 and Escherichia coli (E. coli) ATCC25922 was reduced 2-fold compared to 1018K11. Mechanism exploration suggested that 1018KI11 was more effective than 1018K11 in disrupting the cell barrier and damaging genomic DNA. Additionally, 1018KI11 at certain concentration conditions (2−64 μg/mL) reduced biofilm development of MRSA ATCC43300 by 4.9−85.9%. These data indicated that novel peptide 1018KI11 is a potential food preservative candidate.

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Characterisation of cell membrane interaction mechanisms of antimicrobial peptides by electrical bilayer recording

Cited by 16 publications

References 41 publications

Site-Specific Isopeptide Bond Formation: A Powerful Tool for the Generation of Potent and Nontoxic Antimicrobial Peptides

Site-Specific Isopeptide Bond Formation: A Powerful Tool for the Generation of Potent and Nontoxic Antimicrobial Peptides

WMR Peptide as Antifungal and Antibiofilm against Albicans and Non-Albicans Candida Species: Shreds of Evidence on the Mechanism of Action

Design of a Novel Lysine Isopeptide 1018KI11 with Potent Antimicrobial Activity as a Safe and Stable Food Preservative Candidate

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