Antimicrobial peptides: On future antiprotozoal and anthelminthic applications

Nogrado, Kathyleen; Adisakwattana, Poom; Reamtong, Onrapak

doi:10.1016/j.actatropica.2022.106665

Cited by 8 publications

(4 citation statements)

References 97 publications

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“…The first category focuses on cell wall disruption peptides that can distinguish between bacterial and human or host cells [ 43 , 65 , 66 , 67 ], and their cell wall penetrative properties include the following models: carpet, staves of a barrel, micellar aggregate, and toroidal pores (e.g., magainin-2, protegrin-1) [ 39 , 67 ]. Therefore, with the rise of AMPs in the volume outside the bacterial cells, different reactions eventually lead to the induction of apoptosis (inflammation or electrolyte disequilibrium) [ 62 , 68 ]. The second category of AMPs focuses on non-disruptive cell wall interactions (intracellular targets—altering protein synthesis, enzyme activity, binding, and interfering in DNA and RNA replication) [ 39 , 63 , 67 ].…”

Section: Antimicrobial Peptides (Amps) With Anticancer Potentialmentioning

confidence: 99%

Anticancer Potential of Antimicrobial Peptides: Focus on Buforins

Tolos (Vasii),

Moisa,

Dochia

et al. 2024

Polymers

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In seeking alternative cancer treatments, antimicrobial peptides (AMPs), sourced from various life forms, emerge as promising contenders. These endogenous peptides, also known as host defense peptides (HDPs), play crucial roles in immune defenses against infections and exhibit potential in combating cancers. With their diverse defensive functions, plant-derived AMPs, such as thionins and defensins, offer a rich repertoire of antimicrobial properties. Insects, amphibians, and animals contribute unique AMPs like cecropins, temporins, and cathelicidins, showcasing broad-spectrum activities against bacteria, fungi, and viruses. Understanding these natural peptides holds significant potential for developing effective and targeted therapies against cancer and infectious diseases. Antimicrobial peptides (AMPs) exhibit diverse structural characteristics, including α-helical, β-sheet, extended, and loop peptides. Environmental conditions influence their structure, connecting to changes in cell membrane hydrophobicity. AMPs’ actions involve direct killing and immune regulation, with additional activities like membrane depolarization. In this review, we focus on antimicrobial peptides that act as anticancer agents and AMPs that exhibit mechanisms akin to antimicrobial activity. Buforin AMPs, particularly Buforin I and II, derived from histone H2A, demonstrate antibacterial and anticancer potential. Buforin IIb and its analogs show promise, with selectivity for cancer cells. Despite the challenges, AMPs offer a unique approach to combat microbial resistance and potential cancer treatment. In various cancer types, including HeLa, breast, lung, ovarian, prostate, and liver cancers, buforins demonstrate inhibitory effects and apoptosis induction. To address limitations like stability and bioavailability, researchers explore buforin-containing bioconjugates, covalently linked with nanoparticles or liposomes. Bioconjugation enhances specificity-controlled release and combats drug resistance, presenting a promising avenue for targeted cancer treatment. Clinical translation awaits further evaluation through in vivo studies and future clinical trials.

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Section: Antimicrobial Peptides (Amps) With Anticancer Potentialmentioning

confidence: 99%

Anticancer Potential of Antimicrobial Peptides: Focus on Buforins

Tolos (Vasii),

Moisa,

Dochia

et al. 2024

Polymers

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“…Therefore, numerous investigations have focused on evaluating and characterizing new potential molecules known as antimicrobial peptides (AMPs). These molecules have demonstrated broad biological activity against microbes, fungi, parasite viruses, and in the last decade, cancer cells (Lee et al 2019a ; Li et al 2021 ; Martínez-Culebras et al 2021 ; Nogrado et al 2022 ; Tornesello et al 2020 ). Additionally, it has been demonstrated that these molecules present a mechanism hard to counter that does not allow the bacteria to easily develop resistance pathways, making the peptides potential therapeutic agents for multi-drug resistant bacteria (Zhang and Falla 2006 ).…”

Section: Introductionmentioning

confidence: 99%

Study of the Membrane Activity of the Synthetic Peptide ∆M3 Against Extended-Spectrum β-lactamase Escherichia coli Isolates

Fandiño-Devia,

Santa-González,

Klaiss-Luna

et al. 2024

J Membrane Biol

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Escherichia coli is the most common microorganism causing nosocomial or community-acquired bacteremia, and extended-spectrum β-lactamase-producing Escherichia coli isolates are identified worldwide with increasing frequency. For this reason, it is necessary to evaluate potential new molecules like antimicrobial peptides. They are recognized for their biological potential which makes them promising candidates in the fight against infections. The goal of this research was to evaluate the potential of the synthetic peptide ΔM3 on several extended-spectrum β-lactamase producing E. coli isolates. The antimicrobial and cytotoxic activity of the peptide was spectrophotometrically determined. Additionally, the capacity of the peptide to interact with the bacterial membrane was monitored by fluorescence microscopy and infrared spectroscopy. The results demonstrated that the synthetic peptide is active against Escherichia coli isolates at concentrations similar to Meropenem. On the other hand, no cytotoxic effect was observed in HaCaT keratinocyte cells even at 10 times the minimal inhibitory concentration. Microscopy results showed a permeabilizing effect of the peptide on the bacteria. The infrared results showed that ΔM3 showed affinity for the lipids of the microorganism’s membrane. The results suggest that the ∆M3 interacts with the negatively charged lipids from the E. coli by a disturbing effect on membrane. Finally, the secondary structure experiments of the peptide showed a random structure in solution that did not change during the interaction with the membranes. Graphic Abstract

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“…These molecules have demonstrated broad biological activity against microbes, fungi, parasite viruses, and in the last decade, cancer cells (25,28,32,34,58). Additionally, it has been demonstrated that these molecules present a mechanism hard to counter that does not allow the bacteria to easily develop resistance pathways, making the peptides potential therapeutic agents for multi-drug resistant bacteria (67).…”

Section: Introductionmentioning

confidence: 99%

Study of the Membrane Activity of the Synthetic Peptide ∆M3 against Extended-Spectrum β-Lactamase Escherichia coli Isolates

Fandiño-Devia,

Santa-González,

Klaiss-Luna

et al. 2023

Preprint

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Escherichia coli is the most common microorganism causing nosocomial or community-acquired bacteremia, and extended-spectrum β-lactamase-producing Escherichia coliisolates are identified worldwide with increasing frequency. For this reason, it is necessary to evaluate potential new molecules like antimicrobial peptides. They are recognized for their biological potential which makes them promising candidates in the fight against infections. The goal of this research was to evaluate the potential of the synthetic peptide ΔM3 on several extended-spectrum β-lactamase producing E. coli isolates. The antimicrobial and cytotoxic activity of the peptide spectrophotometrically determined. Additionally, the capacity of the peptide to interact with the bacterial membrane was monitored by fluorescence microscopy and infrared spectroscopy. The results demonstrated that the peptide is active against Escherichia coli isolates at concentrations similar to Meropenem. On the other hand, no cytotoxic effect was observed in keratinocyte cells even at 10 times the minimal inhibitory concentration. Microscopy results showed a permeabilizing effect of the peptide on the bacteria. The infrared results showed that ΔM3 showed affinity for the lipids of the microorganism's membrane. Finally, the peptide showed a random structure in solution that did not change during the interaction with the membranes. The synthetic peptide ΔM3 was demonstrated to have potential antimicrobial activity against β-lactamase-producing E. coli isolates, and low cytotoxicity against HaCaT cells. The results suggest that the ∆M3 interacts with the negatively charged lipids from the E. coli by a disturbing effect on membrane. The secondary structure showed no conformational change for ∆M3.

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Antimicrobial peptides: On future antiprotozoal and anthelminthic applications

Cited by 8 publications

References 97 publications

Anticancer Potential of Antimicrobial Peptides: Focus on Buforins

Anticancer Potential of Antimicrobial Peptides: Focus on Buforins

Study of the Membrane Activity of the Synthetic Peptide ∆M3 Against Extended-Spectrum β-lactamase Escherichia coli Isolates

Study of the Membrane Activity of the Synthetic Peptide ∆M3 against Extended-Spectrum β-Lactamase Escherichia coli Isolates

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