Insights into the membrane interaction mechanism and antibacterial properties of chensinin-1b

Sun, Yue; Dong, Weibing; Sun, Lijun; Ma, Li; Shang, Dejing

doi:10.1016/j.biomaterials.2014.10.041

Cited by 79 publications

(61 citation statements)

References 51 publications

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“…AMPs exhibit a wide range of antibacterial activities through direct electrostatic bonding to the anionic surfaces of bacteria, leading to the disruption of their plasma membrane (6). Furthermore, recent studies have reported that AMPs exhibit anti-tumor activity (7)(8)(9).…”

Section: Introductionmentioning

confidence: 99%

Bovine lactoferricin P13 triggers ROS-mediated caspase-dependent apoptosis in SMMC7721 cells

Meng

et al. 2016

Oncology Letters

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Abstract. Bovine lactoferricin P13 (LfcinB-P13) is a peptide derived from LfcinB. In the present study, the effect of LfcinB-P13 on the human liver cancer cell line SMMC7721 was investigated in vitro and in vivo. The results of the present study indicate that LfcinB-P13 significantly decreased SMMC7721 cell viability in vitro (P=0.032 vs. untreated cells), while exhibiting low cytotoxicity in the wild-type liver cell line L02. In addition, the rate of apoptosis in SMMC7721 cells was significantly increased following treatment with 40 and 60 µg/ml LfcinB-P13 (P=0.0053 vs. the control group), which was associated with an increase in the level of reactive oxygen species (ROS) and the activation of caspase-3 and -9. Furthermore, ROS chelation led to the suppression of LfcinB-P13-mediated caspase-3 and -9 activation in SMMC7721 cells. LfcinB-P13 was demonstrated to markedly inhibit tumor growth in an SMMC7721-xenograft nude mouse model. The results of the present study indicate that LfcinB-P13 is a novel candidate therapeutic agent for the treatment of liver cancer.

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Section: Introductionmentioning

confidence: 99%

Bovine lactoferricin P13 triggers ROS-mediated caspase-dependent apoptosis in SMMC7721 cells

Meng

et al. 2016

Oncology Letters

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“…AMPs initially bind to the negatively charged bacterial cell membrane through electrostatic interactions. Next, they insert themselves into the hydrophobic core and perturb its structure, resulting in an increase in bacterial membrane permeability; the subsequent leakage of cytoplasmic components leads to the death of the microorganism . We previously identified and reported a novel AMP, chensinin‐1, that was isolated and purified from skin secretions of the Chinese brown frog Rana chensinensis .…”

Section: Introductionmentioning

confidence: 99%

Interactions between chensinin‐1, a natural antimicrobial peptide derived from Rana chensinensis, and lipopolysaccharide

2015

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Lipopolysaccharide (LPS) plays a critical role in the pathogenesis of sepsis caused by gram-negative bacterial infections. Therefore, LPS-neutralizing molecules would have important clinical applications. Chensinin-1, a novel antimicrobial peptide with atypical structural features, was found in the skin secretions of the Chinese brown frog Rana chensinensis. To understand the role of LPS in the bacterial susceptibility to chensinin-1 and to investigate its anti-endotoxin effects, the interactions of chensinin-1 with LPS were investigated in this study using circular dichroism, in situ IR, isothermal titration calorimetry, and zeta potential. This study is the first to use in situ IR spectroscopy to evaluate the secondary structural changes of this peptide. The capacity of chensinin-1 to block the LPS-dependent cytokine secretion of macrophages was also investigated. Our results show that chensinin-1 can form α-helical structures in LPS suspensions. LPS can affect the antimicrobial activity of chensinin-1, and chensinin-1 was able to mitigate the effects of LPS. These data may facilitate the development of antimicrobial peptides with potent antimicrobial and anti-endotoxin activities.

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“…AMPs serve as a first line of innate immunity and protect the host by exhibiting potent antimicrobial activity against bacteria, fungi and viruses8. The mode of action is initiated through electrostatic interactions, causing the adsorption of AMPs at the surface of the negatively charged cell membrane910. The majority of AMPs interfere with membrane permeabilization and membrane-associated enzymes by inserting into the outer membrane hydrophobic core and disrupting the bacterial membrane, leading to cell death1112.…”

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confidence: 99%

“…In addition to this direct antimicrobial activity, many AMPs often display immunomodulatory activities, such as chemokine induction and endotoxin neutralization to inhibit lipopolysaccharide (LPS)-induced pro-inflammatory cytokine production1516. In addition, AMPs also exhibit other biological properties, including the stimulation of angiogenesis, which results in immuno-based anti-infection activity in animal models, and the induction of wound repair1017. Taken together, AMPs are the most promising compounds for the development of novel antibiotics18.…”

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confidence: 99%

“…Previous studies indicated that the introduction of Trp residues can significantly improve the antimicrobial activity of the peptide against the Gram-negative bacteria, such as the design of the peptide of IK-6 analogues and chensinin-1b1024. In this study, to improve the antimicrobial and anti-inflammatory activities of chensinin-1 and to better understand the specific biology function of His residues in the sequence of chensinin-1, we replaced three Gly residues with Trp to improve the hydrophobicity of the peptide and obtained the novel mutant peptide MC1-1.…”

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confidence: 99%

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Antimicrobial and anti-inflammatory activities of three chensinin-1 peptides containing mutation of glycine and histidine residues

Dong

Mao

Guan

et al. 2017

Sci Rep

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The natural peptide chensinin-1 doesnot exhibit its desired biological properties. In this study, the mutant MC1-1 was designed by replacing Gly in the chensinin-1 sequence with Trp. Mutants MC1-2 and MC1-3 were designed based on the MC1-1 sequence to investigate the specific role of His residues. The mutated peptides presented α-helicity in a membrane-mimetic environment and exhibited broad-spectrum antimicrobial activities; in contrast to Trp residues, His residues were dispensable for interacting with the cell membrane. The interactions between the mutant peptides and lipopolysaccharide (LPS) facilitated the ingestion of peptides by Gram-negative bacteria. The binding affinities of the peptides were similar, at approximately 10 μM, but ΔH for MC1-2 was −7.3 kcal.mol−1, which was 6-9 folds higher than those of MC1-1 and MC1-3, probably due to the conformational changes. All mutant peptides demonstrated the ability to inhibit LPS-induced tumour-necrosis factor-α (TNF-α) and interleukin-6 (IL-6) release from murine RAW264.7 cells. In addition, the representative peptide MC1-1showed better inhibition of serum TNF-α and IL-6 levels compared to polymyxin B (PMB), a potent binder and neutralizer of LPS as positive control in LPS-challenged mice model. These data suggest that the mutant peptides could be promising molecules for development as chensinin-based therapeutic agents against sepsis.

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Insights into the membrane interaction mechanism and antibacterial properties of chensinin-1b

Cited by 79 publications

References 51 publications

Bovine lactoferricin P13 triggers ROS-mediated caspase-dependent apoptosis in SMMC7721 cells

Bovine lactoferricin P13 triggers ROS-mediated caspase-dependent apoptosis in SMMC7721 cells

Interactions between chensinin‐1, a natural antimicrobial peptide derived from Rana chensinensis, and lipopolysaccharide

Antimicrobial and anti-inflammatory activities of three chensinin-1 peptides containing mutation of glycine and histidine residues

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