Peptides with Dual Antimicrobial-Anticancer Activity Derived from the N-terminal Region of H. pylori Ribosomal Protein L1 (RpL1)

Yaghoubi, Atieh; Khazaei, Majid; Ghazvini, Kiarash; Movaqar, Aref; Hasanian, Seyed Mahdi; Soleimanpour, Saman

doi:10.1007/s10989-020-10150-3

Cited by 7 publications

(2 citation statements)

References 61 publications

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“…One possible application is that of RP eL39 (PaDBS1R1), a synthesized peptide with potential application as a therapeutic antimicrobial agent [ 74 , 76 ]. RP uL1 in H. pylori has also demonstrated strong anticancer and antibacterial activities, as well as antifungal and anti-parasitic activities [ 84 ]. Another RP is the RP uL1 produced from B. tequilensis , which showed anticancer properties, highlighting its advantage for use in selective toxicity against cancerous cells [ 61 ].…”

Section: Applications Of Ampsmentioning

confidence: 99%

Ribosomes: The New Role of Ribosomal Proteins as Natural Antimicrobials

Hurtado-Rios

Carrasco-Navarro

Almanza-Perez

et al. 2022

IJMS

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Moonlighting proteins are those capable of performing more than one biochemical or biophysical function within the same polypeptide chain. They have been a recent focus of research due to their potential applications in the health, pharmacological, and nutritional sciences. Among them, some ribosomal proteins involved in assembly and protein translation have also shown other functionalities, including inhibiting infectious bacteria, viruses, parasites, fungi, and tumor cells. Therefore, they may be considered antimicrobial peptides (AMPs). However, information regarding the mechanism of action of ribosomal proteins as AMPs is not yet fully understood. Researchers have suggested that the antimicrobial activity of ribosomal proteins may be associated with an increase in intracellular reactive oxidative species (ROS) in target cells, which, in turn, could affect membrane integrity and cause their inactivation and death. Moreover, the global overuse of antibiotics has resulted in an increase in pathogenic bacteria resistant to common antibiotics. Therefore, AMPs such as ribosomal proteins may have potential applications in the pharmaceutical and food industries in the place of antibiotics. This article provides an overview of the potential roles of ribosomes and AMP ribosomal proteins in conjunction with their potential applications.

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Section: Applications Of Ampsmentioning

confidence: 99%

Ribosomes: The New Role of Ribosomal Proteins as Natural Antimicrobials

Hurtado-Rios

Carrasco-Navarro

Almanza-Perez

et al. 2022

IJMS

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“…This general mechanism may apply to multiple AMPs. Yaghoubi et al (2021) found that a novel antimicrobial peptide likewise increases the permeability of bacteria and cancer cell membranes, thereby killing these cells. Additional studies of these mechanisms would be illuminating.…”

Section: Discussionmentioning

confidence: 99%

Functional characterization, antimicrobial effects, and potential antibacterial mechanisms of new mastoparan peptides from hornet venom (Vespa ducalis, Vespa mandarinia, and Vespa affinis)

Wen

Gongpan

Meng

et al. 2021

Toxicon

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Antibiotic-resistant bacteria are a major threat to global public health, and there is an urgent need to find effective, antimicrobial treatments that can be well tolerated by humans. Hornet venom is known to have antimicrobial properties, and contains peptides with similarity to known antimicrobial eptides (AMPs), mastoparans. We identified multiple new AMPs from the venom glands of Vespa ducalis (U-VVTX-Vm1a, U-VVTX-Vm1b, and U-VVTX-Vm1c), Vespa mandarinia (U-VVTX-Vm1d), and Vespa affinis (U-VVTX-Vm1e). All of these AMPs have highly similar sequences and are related to the toxic peptide, mastoparan. Our newly identified AMPs have α-helical structures, are amphiphilic, and have antimicrobial properties. Both U-VVTX-Vm1b and U-VVTX-Vm1e killed bacteria, Staphylococcus aureus ATCC25923 and Escherichia coli ATCC25922, at the concentrations of 16 μg/mL and 32 μg/mL, respectively. None of the five AMPs exhibited strong toxicity as measured via their hemolytic activity on red blood cells. U-VVTX-Vm1b was able to increase the permeability of E. coli ATCC25922 and degrade its genomic DNA. These results are promising, demonstrate the value of investigating hornet venom as an antimicrobial treatment, and add to the growing arsenal of such naturally derived treatments.

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