The Remarkable Cationic Peptides: A Boon to Pharmaceutical Sciences?

Omar, Ruchi; Yadav, Arpita

doi:10.18433/jpps29455

Cited by 4 publications

(2 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Plantaricin can inhibit bacterial growth through the mechanism of electrolyte efflux, disrupt membrane potential (Zhang et al 2015), and inhibit the 14-α demethylase enzyme (Omar and Yadav 2018). Plantaricin S34 crude protein has better activity than ampicillin in inhibiting EPEC K1.1.…”

Section: Discussionmentioning

confidence: 99%

Short Communication: Acute toxicity study of plantaricin from Lactobacillus plantarum S34 and its antibacterial activity

et al. 2020

View full text Add to dashboard Cite

Abstract. Ahaddin AY, Budiarti S, Mustopa AZ, Darusman HS, Triratna L. 2021. Short Communication: Acute toxicity study of plantaricin from Lactobacillus plantarum S34 and its antibacterial activity. Biodiversitas 22: 227-232. Lactobacillus plantarum S34 belongs to the Lactobacilli class produces a bacteriocin called plantaricin. Bacteriocins are well known as active compounds that inhibit bacterial growth. This study was conducted to determine the antimicrobial activity of plantaricin S34 and its safety profile in the ddY mouse animal models. Plantaricin 34 from the crude extract was identified using Tricine SDS-PAGE. Antimicrobial activity was observed using disk diffusion against EPEC K1.1, S. aureus, S. typhosa, S typhimurium, and Proteus sp. The safety assessment showed that crude extract of plantaricin S34 did not cause any abnormalities to experimental mice even after being administrated with 5000 mg/kg BB. The identification of plantaricin S34 showed an active molecule at 7.34 kDa and had an activity to inhibit the pathogens used in this study. The blood analysis showed that the hematological and biochemical blood properties were in the normal range. Histopathological examination showed no damage to the intestine, liver, and kidneys. Thus, the crude extract of plantaricin S34 is active as an antimicrobial agent without any toxicity effects.

show abstract

Section: Discussionmentioning

confidence: 99%

Short Communication: Acute toxicity study of plantaricin from Lactobacillus plantarum S34 and its antibacterial activity

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Furthermore, cpps usually contain short sequences with a positive charge resulting from several lysine and arginine residues, and are able both to deliver themselves and to deliver large micromolecules 4. In addition, some cationic anti-microbial peptides (CAMPs), that have some similar physicochemical properties to cpps, can also have cell-penetrating properties, suggesting that they could be highly efficient therapeutic tools 5,6. CAMPs, such as the unique anti-microbial human cathelicidin LL37 peptide, are naturally produced by the innate immune system and mediate a widespread anti-microbial activity against Gram-positive and Gram-negative bacteria such as Staphylococcus aureus and Escherichia coli , and also against fungi and enveloped viruses 7,8.…”

Section: Introductionmentioning

confidence: 99%

<p>Antitumor and antibacterial properties of virally encoded cationic sequences</p>

Colle

Périchon

García

2019

BTT

View full text Add to dashboard Cite

Objective: The objective of this study was to test our Viral Quinta Columna Strategy (VQCS), a new biological hypothesis predicting that specific multifunctional virally encoded cationic domains may have the capacity to penetrate human cells and interact with PP2A proteins to deregulate important human intracellular pathways, and may display LL37 cathelicidin-like antagonistic effects against multiple pathogens such as bacteria or viruses. Methods: We comparatively analyzed the host defense properties of adenodiaphorins and of some specific cationic sequences encoded by different viruses using two distinct biological models: U87G, a well-characterized cell tumor model; and a group B Streptococcus agalactiae NEM316 ΔdltA, highly sensitive to LL37 cathelicidin. Results: We found that the adenovirus type 2 E4orf4 is a cell-permeable protein containing a new E4orf4 64–95 protein transduction domain, named large adenodiaphorin or LadD 64–95 . Interestingly, the host defense LL37 peptide is the unique cathelicidin in humans. In this context, we also demonstrated that similarly to LL37 LadD 64–95 , several virally encoded cationic sequences including the C-terminus HIV-1 89.6 Vpr 77–92 , shorter adenodiaphorins AdD 67–84 /AdD/ 69–84 /AdD 69–83 , as well as HIV-2 Tat 67–90 and JC polyomavirus small t 115–134 , displayed similar toxicity against Gram-positive S. agalactiae NEM316 ΔdltA strain. Finally, LadD 64–95 , adenodiaphorin AdD 67–84 , AdD 69–84 , and LL37 and LL 17–32 cathelicidin peptides also inhibited the survival of human U87G glioblastoma cells. Conclusion: In this study, we demonstrated that specific cationic sequences encoded by four different viruses displayed antibacterial activities against S. agalactiae NEM316 ΔdltA strain. In addition, HIV-1 Vpr 71–92 and adenovirus 2 E4orf4 64–95, two cationic penetrating sequences that bind PP2A, inhibited the survival of U87G glioblastoma cells. These results illustrate the host defense properties of virally encoded sequences and could represent an initial step for future complete validation of the VQCS hypothesis.

show abstract

A Comparative Study of the Antimicrobial and Structural Properties of Short Peptides and Lipopeptides Containing a Repetitive Motif KLFK

Húmpola

Rey

Spontón

et al. 2019

PPL

View full text Add to dashboard Cite

Background: In the last years, Antimicrobial Peptides (AMPs) and lipopeptides have received attention as promising candidates to treat infections caused by resistant microorganisms. </P><P> Objective: The main objective of this study was to investigate the effect of repetitive KLFK motifs and the attachment of aliphatic acids to the N-terminus of (KLFK)n peptides on therapeutic properties. Methods: Minimal inhibitory concentration against Gram (+) and (-) bacteria and yeast of synthetic compounds were determined by broth microtiter dilution method, and the toxicity was evaluated by hemolysis assay. Membrane-peptide interaction studies were performed with model phospholipid membranes mimicking those of bacterial and mammalian cells by Fluorescence Spectroscopy. The secondary structure in solution and membranes was determined by Circular Dichroism. Results: Our results showed that the resulting compounds have inhibitory activity against bacteria and fungi. The (KLFK)3 peptide showed the highest therapeutic index against bacterial and yeast strains, and the (KLFK)2 peptide conjugated with octanoic acid was the most active against yeasts. All the lipopeptides containing long-chain fatty acids (C14 or longer) were highly hemolytic at low concentrations. The antimicrobial activity of (KLFK)2 and (KLFK)3 lipopeptides was mainly associated with improved stability of the amphipathic secondary structure, which showed high contributions of α-helix in dipalmitoylphosphatidylglycerol (DPPG) vesicles. Conclusion: The repetition of the KLFK sequence and the conjugation with lipid tails allowed obtained compounds with high antimicrobial activity and low toxicity, becoming good candidates for treating infectious diseases.

show abstract

The Remarkable Cationic Peptides: A Boon to Pharmaceutical Sciences?

Cited by 4 publications

References 44 publications

Short Communication: Acute toxicity study of plantaricin from Lactobacillus plantarum S34 and its antibacterial activity

Short Communication: Acute toxicity study of plantaricin from Lactobacillus plantarum S34 and its antibacterial activity

<p>Antitumor and antibacterial properties of virally encoded cationic sequences</p>

A Comparative Study of the Antimicrobial and Structural Properties of Short Peptides and Lipopeptides Containing a Repetitive Motif KLFK

Contact Info

Product

Resources

About