Identification and target-modifications of temporin-PE: A novel antimicrobial peptide in the defensive skin secretions of the edible frog, Pelophylax kl. esculentus

Sang, Mengru; Wu, Qinan; Xi, Xinping; Ma, Chengbang; Wang, Lei; Burrows, James F.; Chen, Tianbao

doi:10.1016/j.bbrc.2017.11.173

Cited by 13 publications

(17 citation statements)

References 33 publications

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“…AMPs have also shown great potential as new anticancer therapeutics [ 18 , 19 ], and here indeed, R2PLx can potently inhibit the proliferation of tumour cells. It is generally proposed that the antiproliferative mechanism of AMPs on cancer cells is similar to their antimicrobial action, based upon the observation that tumour cells can also possess a negatively charged membrane [ 20 ].…”

Section: Discussionmentioning

confidence: 99%

A novel antimicrobial peptide, Ranatuerin-2PLx, showing therapeutic potential in inhibiting proliferation of cancer cells

Chen

Zhang

et al. 2018

Bioscience Reports

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Antimicrobial peptides are a promising resource for developing novel antibiotic and even anticancer drugs. Here, a 28-mer polypeptide, Ranatuerin-2PLx (R2PLx), was identified from lyophilised skin secretions. The chemically synthetic replicates exhibited moderate and broadspectrum antimicrobial effect against various microorganisms including methicillin-resistant Staphylococcus aureus (MRSA, minimal inhibitory concentration = 256 µM). In addition, R2PLx was found to inhibit the proliferation of several tumour cells, especially showing more potent effect on prostate cancer cell, PC-3. The early cell apoptosis was observed in 6 h by Annexin V-FITC/propidium iodide staining, as well as the activation of Caspase-3 at 5 µM peptide concentration. R2PLx may therefore be promising for developing new therapeutic approach for cancer treatment. Moreover, the artificial deficiency of conserved rana-box loop or net positive charge in C-terminal domain notably reduced the biological activities of the truncated and substituted isoforms, respectively, suggesting for maintaining their biological potency of ranatuerin family requires both cysteine-bridged segment and cationincity within the loop domain in C-terminus.

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Section: Discussionmentioning

confidence: 99%

A novel antimicrobial peptide, Ranatuerin-2PLx, showing therapeutic potential in inhibiting proliferation of cancer cells

Chen

Zhang

et al. 2018

Bioscience Reports

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“…Sang et al [45] have extracted from the secretion of Pelophylax kl. esculentus skin the temporin-PE, a potent AMP (Table 1).…”

Section: Antimicrobial Peptides As Anti-biofilm Agentsmentioning

confidence: 99%

Biofilms: Novel Strategies Based on Antimicrobial Peptides

et al. 2019

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The problem of drug resistance is very worrying and ever increasing. Resistance is due not only to the reckless use of antibiotics but also to the fact that pathogens are able to adapt to different conditions and develop self-defense mechanisms such as living in biofilms; altogether these issues make the search for alternative drugs a real challenge. Antimicrobial peptides appear as promising alternatives but they have disadvantages that do not make them easily applicable in the medical field; thus many researches look for solutions to overcome the disadvantages and ensure that the advantages can be exploited. This review describes the biofilm characteristics and identifies the key features that antimicrobial peptides should have. Recalcitrant bacterial infections caused by the most obstinate bacterial species should be treated with a strategy to combine conventional peptides functionalized with nano-tools. This approach could effectively disrupt high density infections caused by biofilms. Moreover, the importance of using in vivo non mammalian models for biofilm studies is described. In particular, here we analyze the use of amphibians as a model to substitute the rodent model.

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“…We tested the hemolytic activity of the peptides in the presence and absence of S. aureus . GHa and derived peptides showed lower hemolytic activity than temporin 1Ga (HL 50 = 12.5 μM), temporin-PE (HL 50 = 39.64 μM) and melittin (HL 50 = 2.5 μM) [24,31,47]. Moreover, the TI of the derived peptides increased by 4–8 times and the CSI increased by 2–4 times.…”

Section: Discussionmentioning

confidence: 99%

“…The GHa cloned by our laboratory was used as a template for designing a series of analogs. GHa is similar to most temporin peptides such as temporin 1Tb, temporin-PE [30,31], and showing potent activity against Gram-positive bacteria instead of Gram-negative bacteria. In order to improve the therapeutic potential of GHa, we designed three derived peptides GHaK, GHa4K, and GHa11K.…”

Section: Discussionmentioning

confidence: 99%

The Analogs of Temporin-GHa Exhibit a Broader Spectrum of Antimicrobial Activity and a Stronger Antibiofilm Potential against Staphylococcus aureus

et al. 2019

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The abuse of antibiotics has led to the emergence of multidrug-resistant bacteria, which is becoming a serious worldwide problem people have to face. In our previous study, temporin-GHa (GHa) cloned from Hylarana guentheri showed antimicrobial activity against Gram-positive bacteria. In order to improve its therapeutic potential, we used a template-based and a database-assisted design to obtain three derived peptides by replacing the histidine at both ends of GHa with lysine, which exhibited faster and stronger bactericidal activity and a broader spectrum than the parent peptide. GHaK and GHa4K targeted to the bacterial membrane to exert their antibacterial activities at a faster membrane damage rate. The derived peptides inhibited the initial adhesion and the formation of Staphylococcus aureus biofilms, and eradicated the mature biofilms, which indicated that the derived peptides effectively penetrated the biofilm and killed bacteria. The therapeutic index (TI) and cell selectivity index (CSI) of the derived peptides increased significantly, which means a broader therapeutic window of the derived peptides. The derived peptides with improved activity and cell selectivity have the potential to be the promising candidates for the treatment of S. aureus infections. Our research also provides new insights into the design and development of antimicrobial peptides.

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Identification and target-modifications of temporin-PE: A novel antimicrobial peptide in the defensive skin secretions of the edible frog, Pelophylax kl. esculentus

Cited by 13 publications

References 33 publications

A novel antimicrobial peptide, Ranatuerin-2PLx, showing therapeutic potential in inhibiting proliferation of cancer cells

A novel antimicrobial peptide, Ranatuerin-2PLx, showing therapeutic potential in inhibiting proliferation of cancer cells

Biofilms: Novel Strategies Based on Antimicrobial Peptides

The Analogs of Temporin-GHa Exhibit a Broader Spectrum of Antimicrobial Activity and a Stronger Antibiofilm Potential against Staphylococcus aureus

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