Antimicrobial peptides with anticancer activity: Today status, trends and their computational design

Kordi, Masoumeh; Borzouyi, Zeynab; Chitsaz, Saideh; Salami, Robab; Tabarzad, Maryam

doi:10.1016/j.abb.2022.109484

Cited by 29 publications

(18 citation statements)

References 108 publications

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“…[39,40] Due to the changes in the tumor microenvironment, the PS is exposed and the plasma membrane becomes negatively charged, creating a favorable space for the interaction between the tumor membrane and the peptide. [32,41] This change in membrane charge also contributes to the selectivity of peptides to interact with cancer cells since the electrostatic attraction will be stronger than normal cells. Moreover, the use of antimicrobial peptides in anticancer therapy becomes a possibility to detect cells that are not yet metabolically active but already have an altered microenvironment, [33] as well as an alternative for cases of microbial resistance to antibiotics.…”

Section: Repositioning Antimicrobial Peptides For Cancer Treatmentmentioning

confidence: 99%

“…Due to the changes in the tumor microenvironment, the PS is exposed and the plasma membrane becomes negatively charged, creating a favorable space for the interaction between the tumor membrane and the peptide [32,41] . This change in membrane charge also contributes to the selectivity of peptides to interact with cancer cells since the electrostatic attraction will be stronger than normal cells.…”

Section: Repositioning Antimicrobial Peptides For Cancer Treatmentmentioning

confidence: 99%

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Recalculating the Route: Repositioning Antimicrobial Peptides for Cancer Treatment

de Almeida Gomes,

da Lima,

da Silva Brito

et al. 2023

Chemistry & Biodiversity

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Resistance to antimicrobial drugs has been considered a public health problem. Likewise, the increasing resistance of cancer cells to drugs currently used in therapy has also become a problem. Therefore, the research and development of synthetic peptides bring a new perspective on the emergence of new drugs for treating this resistance since bioinformatics provides a means to optimize these molecules and save time and costs in research. Peptides have several mechanisms of action, such as forming pores on the cell membrane and inhibiting protein synthesis. Some studies report the use of antimicrobial peptides with the potential for action against cancer cells, suggesting a repositioning of antimicrobial peptides to fight back cancer resistance. There is an alteration in the microenvironment, making its net charge negative for the survival and growth of cancer cells. The changes in glycoproteins favor the membrane to have a more negative charge, favoring the interaction between the cells and the peptide, thus making possible the repositioning of these antimicrobial peptides against cancer. Here, we will discuss the mechanism of action, targets and effects of peptides, comparison between microbial and cancer cells, and proteomic changes caused by the interaction of peptides and cells.

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Section: Repositioning Antimicrobial Peptides For Cancer Treatmentmentioning

confidence: 99%

Section: Repositioning Antimicrobial Peptides For Cancer Treatmentmentioning

confidence: 99%

Recalculating the Route: Repositioning Antimicrobial Peptides for Cancer Treatment

de Almeida Gomes,

da Lima,

da Silva Brito

et al. 2023

Chemistry & Biodiversity

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“…Apart from this serious problem, cancer also represents a global health concern worldwide: it has been reported that cancer caused 10 million deaths in 2020 [ 5 ], and this number is forecasted to exceed 13 million by 2030 [ 6 ]. The main limitation in the pharmacological treatment of various tumoral diseases is the resistance of cancer cells to conventional chemotherapeutic agents [ 7 ]. Hence, there is an urgent necessity to develop new drugs to overcome bacterial and cancer resistance, with high selectivity and an absence of adverse effects on normal cells [ 8 , 9 ].…”

Section: Introductionmentioning

confidence: 99%

“…To date, several AMPs and ACPs have been isolated from various natural sources such as insects and amphibians [ 7 ], although it is difficult to achieve representative quantities of peptides with the required purity for application in scientific and therapeutic research. Thus, the production of synthetic AMPs and ACPs represents a prominent strategy in the development of novel AMPs and ACPs with a wide range of bioactivities [ 18 , 19 ].…”

Section: Introductionmentioning

confidence: 99%

New Bioactive Peptides from the Mediterranean Seagrass Posidonia oceanica (L.) Delile and Their Impact on Antimicrobial Activity and Apoptosis of Human Cancer Cells

Punginelli

Catania

Abruscato

et al. 2023

IJMS

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The demand for new molecules to counter bacterial resistance to antibiotics and tumor cell resistance is increasingly pressing. The Mediterranean seagrass Posidonia oceanica is considered a promising source of new bioactive molecules. Polypeptide-enriched fractions of rhizomes and green leaves of the seagrass were tested against Gram-positive (e.g., Staphylococcus aureus, Enterococcus faecalis) and Gram-negative bacteria (e.g., Pseudomonas aeruginosa, Escherichia coli), as well as towards the yeast Candida albicans. The aforementioned extracts showed indicative MIC values, ranging from 1.61 μg/mL to 7.5 μg/mL, against the selected pathogens. Peptide fractions were further analyzed through a high-resolution mass spectrometry and database search, which identified nine novel peptides. Some discovered peptides and their derivatives were chemically synthesized and tested in vitro. The assays identified two synthetic peptides, derived from green leaves and rhizomes of P. oceanica, which revealed interesting antibiofilm activity towards S. aureus, E. coli, and P. aeruginosa (BIC50 equal to 17.7 μg/mL and 70.7 μg/mL). In addition, the natural and derivative peptides were also tested for potential cytotoxic and apoptosis-promoting effects on HepG2 cells, derived from human hepatocellular carcinomas. One natural and two synthetic peptides were proven to be effective against the “in vitro” liver cancer cell model. These novel peptides could be considered a good chemical platform for developing potential therapeutics.

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“…In the presence of small headgroups, such as ethanolamine of PE, the amphipathic peptide may even stabilize the bilayer properties by intercalation. However, at high peptide-to-lipid ratios, the peptide tends to cover the surface (carpet model) causing the formation of transient micro-sized pores [ 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 , 43 , 44 , 45 ] that allow the transmembrane passage of molecules [ 11 , 46 , 47 ]. This is possible because of the “soft” nature of the bilayer which can deform, change its thickness, and adapt to different perturbations [ 48 , 49 ].…”

Section: Introductionmentioning

confidence: 99%

The Mechanism of Action of SAAP-148 Antimicrobial Peptide as Studied with NMR and Molecular Dynamics Simulations

et al. 2023

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Background: SAAP-148 is an antimicrobial peptide derived from LL-37. It exhibits excellent activity against drug-resistant bacteria and biofilms while resisting degradation in physiological conditions. Despite its optimal pharmacological properties, its mechanism of action at the molecular level has not been explored. Methods: The structural properties of SAAP-148 and its interaction with phospholipid membranes mimicking mammalian and bacterial cells were studied using liquid and solid-state NMR spectroscopy as well as molecular dynamics simulations. Results: SAAP-148 is partially structured in solution and stabilizes its helical conformation when interacting with DPC micelles. The orientation of the helix within the micelles was defined by paramagnetic relaxation enhancements and found similar to that obtained using solid-state NMR, where the tilt and pitch angles were determined based on 15N chemical shift in oriented models of bacterial membranes (POPE/POPG). Molecular dynamic simulations revealed that SAAP-148 approaches the bacterial membrane by forming salt bridges between lysine and arginine residues and lipid phosphate groups while interacting minimally with mammalian models containing POPC and cholesterol. Conclusions: SAAP-148 stabilizes its helical fold onto bacterial-like membranes, placing its helix axis almost perpendicular to the surface normal, thus probably acting by a carpet-like mechanism on the bacterial membrane rather than forming well-defined pores.

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Antimicrobial peptides with anticancer activity: Today status, trends and their computational design

Cited by 29 publications

References 108 publications

Recalculating the Route: Repositioning Antimicrobial Peptides for Cancer Treatment

Recalculating the Route: Repositioning Antimicrobial Peptides for Cancer Treatment

New Bioactive Peptides from the Mediterranean Seagrass Posidonia oceanica (L.) Delile and Their Impact on Antimicrobial Activity and Apoptosis of Human Cancer Cells

The Mechanism of Action of SAAP-148 Antimicrobial Peptide as Studied with NMR and Molecular Dynamics Simulations

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