Melittin and its potential in the destruction and inhibition of the biofilm formation by Staphylococcus aureus , Escherichia coli and Pseudomonas aeruginosa isolated from bovine milk

Picoli, Tony; Peter, Cristina Mendes; Zani, João Luíz; Waller, Stefanie Bressan; Lopes, Matheus Gomes; Boesche, Kamilla Neutzling; Vargas, Gilberto D’Ávila; Hübner, Sílvia de Oliveira; Fischer, Geferson

doi:10.1016/j.micpath.2017.09.046

Cited by 77 publications

(60 citation statements)

References 36 publications

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“…The hypothesis behind this experiment was that the DNase I would break down the matrix of the biofilm and allow the melittin greater penetration, and therefore give it greater efficacy. Results showed that melittin was not an effective treatment for E. coli biofilms, in contrast to previous literature(Picoli et al, 2017), but that DNase I potentially was. A possible reason for the DNase I being significantly different from the melittin but not from the buffer is that when sub-inhibitory concentrations of treatments were applied to biofilms, they can actually slightly promote biofilm growth (Picoli et al, 2017; Jolivet-Gougeon & Bonnaure-Mallet, 2014).…”

Section: Discussioncontrasting

confidence: 98%

“…Results showed that melittin was not an effective treatment for E. coli biofilms, in contrast to previous literature(Picoli et al, 2017), but that DNase I potentially was. A possible reason for the DNase I being significantly different from the melittin but not from the buffer is that when sub-inhibitory concentrations of treatments were applied to biofilms, they can actually slightly promote biofilm growth (Picoli et al, 2017; Jolivet-Gougeon & Bonnaure-Mallet, 2014). This result indicates that the melittin concentration could have been too low, which could have been caused by mishandling of the protein.…”

Section: Discussioncontrasting

confidence: 98%

“…The melittin (Sigma-Aldrich) was reconstituted and diluted, using sterile deionized H2O for both processes, to a concentration of 84μg/mL, a value roughly double its minimum inhibitory concentration, and the DNase I treatment was reconstituted using water and diluted using PBS to a concentration of 5μg/mL, based upon data regarding its action against E. coli biofilms in various doses over time (Picoli et al, 2017; Tetz et al, 2009).…”

Section: Methodsmentioning

confidence: 99%

“…Therefore, attempts have been made to design them rationally, in order to optimize their performance and minimize these hindrances (de la Fuente-Núñez et al, 2017). Melittin is one of these antimicrobial peptides; it is found in honey bee venom and works by destabilizing cell membranes, likely through permeabilization, artificial pore formation, disruption and/or lysis (Picoli et al, 2017). It is effective against Escherichia coli biofilms, with an MIC of 40-42.5μg/mL and an MBC of 64-128μg/mL (Picoli et al, 2017).…”

Section: Introductionmentioning

confidence: 99%

“…When antimicrobial peptides are used in combination with antibiotics they have been shown to usually have additive or synergistic effects rather than antagonistic, and that using them in combination decreases their minimum biofilm eradication concentration to clinically manageable levels, making them a promising treatment to test in clinical trials (Dosler & Karaaslan, 2014). Melittin is effective against biofilms, but only in large and expensive concentrations that are not feasible for practical use (Picoli et al, 2017). A way that has been shown to increase the efficacy of antimicrobial peptides against biofilms is the usage of them in combination with other antibiofilm agents, as this can create synergistic effects (Dosler & Karaaslan, 2014).…”

Section: Introductionmentioning

confidence: 99%

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The Efficacy of the Antimicrobial Peptide Melittin and the Enzyme DNase I Against E. coli Biofilms

Phillips

2019

Preprint

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21Biofilms are aggregations of bacteria that often cause nosocomial infections and are tolerant to 22 antibiotic treatments due to a variety of factors, including the physical barrier of their 23 matrix. One field of treatment that has been explored is the use of antimicrobial peptides, like 24 melittin. Melittin has been demonstrated to have antimicrobial effects on bacteria in both a 25 biofilm and a planktonic state. Its required concentration to affect biofilms, however, is too high 26 to be applicable in clinical settings. One potential way to increase efficacy is to use a compound 27 like DNase I that degrades the matrix and thereby increases the penetration of melittin into the 28 biofilm. I investigated whether DNase I would enhance the efficacy of melittin in relatively low 29 concentrations that could be clinically viable. Melittin and DNase I were applied to E. 30 coli biofilms in 24-well plates, both individually and in combination; biofilm density was 31 measured at two time-points afterwards, using a crystal violet staining assay. The results showed 32 DNase I was the most effective treatment. Surprisingly, none of the melittin treatments were 33 statistically significant. A second experiment investigated variation among 11 bioreplicates and 34 found that there was approximately 5-fold variation in response to treatment with DNase 35

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Section: Discussioncontrasting

confidence: 98%

Section: Discussioncontrasting

confidence: 98%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The Efficacy of the Antimicrobial Peptide Melittin and the Enzyme DNase I Against E. coli Biofilms

Phillips

2019

Preprint

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ProT‐Diff: A Modularized and Efficient Strategy for De Novo Generation of Antimicrobial Peptide Sequences by Integrating Protein Language and Diffusion Models

Wang,

Tang,

Sun

et al. 2024

Advanced Science

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Antimicrobial peptides (AMPs) are a promising solution for treating antibiotic‐resistant pathogens. However, efficient generation of diverse AMPs without prior knowledge of peptide structures or sequence alignments remains a challenge. Here, ProT‐Diff is introduced, a modularized deep generative approach that combines a pretrained protein language model with a diffusion model for the de novo generation of AMPs sequences. ProT‐Diff generates thousands of AMPs with diverse lengths and structures within a few hours. After silico physicochemical screening, 45 peptides are selected for experimental validation. Forty‐four peptides showed antimicrobial activity against both gram‐positive or gram‐negative bacteria. Among broad‐spectrum peptides, AMP_2 exhibited potent antimicrobial activity, low hemolysis, and minimal cytotoxicity. An in vivo assessment demonstrated its effectiveness against a drug‐resistant E. coli strain in acute peritonitis. This study not only introduces a viable and user‐friendly strategy for de novo generation of antimicrobial peptides, but also provides potential antimicrobial drug candidates with excellent activity. It is believed that this study will facilitate the development of other peptide‐based drug candidates in the future, as well as proteins with tailored characteristics.

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A rationally engineered small antimicrobial peptide with potent antibacterial activity

Behera,

Ghosh,

Gupta

et al. 2023

J of Cellular Biochemistry

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Antimicrobial resistance (AMR) is a silent pandemic declared by the WHO that requires urgent attention in the post‐COVID world. AMR is a critical public health concern worldwide, potentially affecting people at different stages of life, including the veterinary and agriculture industries. Notably, very few new‐age antimicrobial agents are in the current developmental pipeline. Thus, the design, discovery, and development of new antimicrobial agents are required to address the menace of AMR. Antimicrobial peptides (AMPs) are an important class of antimicrobial agents for combating AMR due to their broad‐spectrum activity and ability to evade AMR through a multimodal mechanism of action. However, molecular size, aggregability, proteolytic degradation, cytotoxicity, and hemolysis activity significantly limit the clinical application of natural AMPs. The de novo design and engineering of a short synthetic amphipathic AMP (≤16 aa, Mol. Wt. ≤ 2 kDa) with an unusual architecture comprised of coded and noncoded amino acids (NCAAs) is presented here, which demonstrates potent antibacterial activity against a few selected bacterial strains mentioned in the WHO priority list. The designer AMP is conformationally ordered in solution and effectively permeabilizes the outer and inner membranes, leading to bacterial growth inhibition and death. Additionally, the peptide is resistant to proteolysis and has negligible cytotoxicity and hemolysis activity up to 150 μM toward cultured human cell lines and erythrocytes. The designer AMP is unique and appears to be a potent therapeutic candidate, which can be subsequently subjected to preclinical studies to explicitly understand and address the menace of AMR.

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Melittin and its potential in the destruction and inhibition of the biofilm formation by Staphylococcus aureus , Escherichia coli and Pseudomonas aeruginosa isolated from bovine milk

Cited by 77 publications

References 36 publications

The Efficacy of the Antimicrobial Peptide Melittin and the Enzyme DNase I Against E. coli Biofilms

The Efficacy of the Antimicrobial Peptide Melittin and the Enzyme DNase I Against E. coli Biofilms

ProT‐Diff: A Modularized and Efficient Strategy for De Novo Generation of Antimicrobial Peptide Sequences by Integrating Protein Language and Diffusion Models

A rationally engineered small antimicrobial peptide with potent antibacterial activity

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