Different Expression Profiles of Bioactive Peptides in<i>Pelophylax nigromaculatus</i>from Distinct Regions

Song, Yuzhu; Ji, Senlin; Liu, Wa; Yu, Xuya; Meng, Qingxiong; Lai, Ren

doi:10.1271/bbb.130044

Cited by 18 publications

(16 citation statements)

References 22 publications

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“…The MICs of three AMPs against Gram-positive bacterial strains ranged from 4 to 64 μM, and those against fungi ranged between 8 and 32 μM. These results concur with the findings of another study on temporin-1KM, with a similar primary structure to temporin-FL, which demonstrated strong activity against S. aureus and C. albicans , with MICs of approximately 4 and 8 μM, respectively ( Song et al, 2013 ). The diverse antimicrobial effects of temporins on different bacteria can be largely attributed to the cell envelopes of the latter.…”

Section: Discussionsupporting

confidence: 88%

Bioevaluation and Targeted Modification of Temporin-FL From the Skin Secretion of Dark-Spotted Frog (Pelophylax nigromaculatus)

Wang

Yang

et al. 2021

Front. Mol. Biosci.

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Bioactive proteins secreted by the granular glands of amphibian skin play a self-defensive role, and exhibit various bioactivities in vitro and in vivo. In light of the severity of the problem of antibiotic resistance for treating infections, many antimicrobial peptides (AMPs) have been developed and applied in clinical microbial treatments. We identified a naturally derived and potent antimicrobial peptide, temporin-FL, obtained from the skin secretion of Pelophylax nigromaculatus via “shotgun” cloning. Two truncated analogues of this peptide were chemically synthesized to explore their structural-functional relationships. The results of a functional evaluation showed that all of the tested AMPs were active against Gram-positive bacteria and fungi and demonstrated antibiofilm activity against methicillin-resistant Staphylococcus aureus (MRSA) but did not have an effect on Gram-negative bacteria. Moreover, temporin-FLa demonstrated a higher level of hydrophobicity and enhanced antimicrobial efficiency, as well as hemolytic activity and cell cytotoxicity than the parent peptide. Temporin-FLb, which evidenced significantly less α-helicity, was less potent against various microbes but exhibited lower cytotoxicity relating to mammalian cells. Both of the synthesized analogues possessed a higher therapeutic index than the original peptide. Moreover, the membrane permeability assay and the measuring membrane depolarization assay declared that temporin-FL and its analogues induced membrane fracture and depolarization; the quantitative biofilm formation assay and the observations of MRSA biofilms using scanning electron microscopy revealed that the AMPs caused biofilm disruption and blocked biofilm formation, the former experiments all confirming their antimicrobial and antibiofilm properties. Hence, the optimization of temporin-FL offers insights for the discovery of new drugs for treating MRSA infections.

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Section: Discussionsupporting

confidence: 88%

Bioevaluation and Targeted Modification of Temporin-FL From the Skin Secretion of Dark-Spotted Frog (Pelophylax nigromaculatus)

Wang

Yang

et al. 2021

Front. Mol. Biosci.

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“…However, amphibian AMPs can have other functions such as anticancer, anti-diabetes, and spermicidal functions ( Table 2 ). The expression of such peptides is not understood, but can depend on pathogen types, amphibian species [ 4 , 51 ], sex [ 130 ], life stages [ 131 ], season [ 130 , 132 ], and geographic regions [ 133 ]. Cultivation of frogs under sterilized conditions reduces AMP expression and can be restored after exposure to the natural environment [ 133 ].…”

Section: Discussionmentioning

confidence: 99%

“…In the APD database, 35% of amphibian AMPs are C-terminally amidated to increase the peptide net charge by +1 (for accuracy, this modification is considered in the APD when calculating the net charge of peptides). C-terminal amidation can be essential for the antimicrobial activity of amphibian peptides [ 133 , 149 ]. A plausible reason is stabilization of the helical structure to allow for the formation of one additional hydrogen bond.…”

Section: Discussionmentioning

confidence: 99%

Bioinformatic Analysis of 1000 Amphibian Antimicrobial Peptides Uncovers Multiple Length-Dependent Correlations for Peptide Design and Prediction

Wang

2020

Antibiotics

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Amphibians are widely distributed on different continents, except for the polar regions. They are important sources for the isolation, purification and characterization of natural compounds, including peptides with various functions. Innate immune antimicrobial peptides (AMPs) play a critical role in warding off invading pathogens, such as bacteria, fungi, parasites, and viruses. They may also have other biological functions such as endotoxin neutralization, chemotaxis, anti-inflammation, and wound healing. This article documents a bioinformatic analysis of over 1000 amphibian antimicrobial peptides registered in the Antimicrobial Peptide Database (APD) in the past 18 years. These anuran peptides were discovered in Africa, Asia, Australia, Europe, and America from 1985 to 2019. Genomic and peptidomic studies accelerated the discovery pace and underscored the necessity in establishing criteria for peptide entry into the APD. A total of 99.9% of the anuran antimicrobial peptides are less than 50 amino acids with an average length of 24 and a net charge of +2.5. Interestingly, the various amphibian peptide families (e.g., temporins, brevinins, esculentins) can be connected through multiple length-dependent relationships. With an increase in length, peptide net charge increases, while the hydrophobic content decreases. In addition, glycine, leucine, lysine, and proline all show linear correlations with peptide length. These correlations improve our understanding of amphibian peptides and may be useful for prediction and design of new linear peptides with potential applications in treating infectious diseases, cancer and diabetes.

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“…The usual nomenclature for new AOPs from frog's skin secretions uses the term "antioxidin" followed by first letter of the two names comprising the specie name (genus plus specific epitope). For example, Song et al [51] described an AOP isolated from Pelophylax nigromaculatus named as antioxidin-PN. Other examples are antioxidin-RL and antioxidin-RP from Odorrana livida and Rana pleuraden, respectively [9,12].…”

Section: Purification and Structural Characterization Of Antioxidinmentioning

confidence: 99%

Structure and function of a novel antioxidant peptide from the skin of tropical frogs

Barbosa

Oliveira

Plácido

et al. 2018

Free Radical Biology and Medicine

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The amphibian skin plays an important role protecting the organism from external harmful factors such as microorganisms or UV radiation. Based on biorational strategies, many studies have investigated the cutaneous secretion of anurans as a source of bioactive molecules. By a peptidomic approach, a novel antioxidant peptide (AOP) with in vitro free radical scavenging ability was isolated from Physalaemus nattereri. The AOP, named antioxidin-I, has a molecular weight [M+H] = 1543.69Da and a TWYFITPYIPDK primary amino acid sequence. The gene encoding the antioxidin-I precursor was expressed in the skin tissue of three other Tropical frog species: Phyllomedusa tarsius, P. distincta and Pithecopus rohdei. cDNA sequencing revealed highly homologous regions (signal peptide and acidic region). Mature antioxidin-I has a novel primary sequence with low similarity compared with previously described amphibian's AOPs. Antioxidin-I adopts a random structure even at high concentrations of hydrophobic solvent, it has poor antimicrobial activity and poor performance in free radical scavenging assays in vitro, with the exception of the ORAC assay. However, antioxidin-I presented a low cytotoxicity and suppressed menadione-induced redox imbalance when tested with fibroblast in culture. In addition, it had the capacity to substantially attenuate the hypoxia-induced production of reactive oxygen species when tested in hypoxia exposed living microglial cells, suggesting a potential neuroprotective role for this peptide.

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Different Expression Profiles of Bioactive Peptides inPelophylax nigromaculatusfrom Distinct Regions

Cited by 18 publications

References 22 publications

Bioevaluation and Targeted Modification of Temporin-FL From the Skin Secretion of Dark-Spotted Frog (Pelophylax nigromaculatus)

Bioevaluation and Targeted Modification of Temporin-FL From the Skin Secretion of Dark-Spotted Frog (Pelophylax nigromaculatus)

Bioinformatic Analysis of 1000 Amphibian Antimicrobial Peptides Uncovers Multiple Length-Dependent Correlations for Peptide Design and Prediction

Structure and function of a novel antioxidant peptide from the skin of tropical frogs

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