Characterization of simplified nonapeptides with broad-spectrum antimicrobial activities as potential food preservatives, and their antibacterial mechanism

Yang, Zhanyi; Wei, Yingxin; Wu, Wanpeng; Zhang, Licong; Wang, Jiajun; Shan, Anshan

doi:10.1039/d2fo03861g

Cited by 10 publications

(4 citation statements)

References 66 publications

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“…Subsequently, chicken breasts were divided into 1 g pieces and put into sterile centrifuge tubes, and the bacterial suspension (1 × 10 4 cfu/mL) was added at a ratio of 500 μL/g, followed by the addition of AMP to achieve a final concentration of 4 × MIC. Finally, all samples were immediately stored at 4 °C for 5 days, and then the number of bacteria in the different treatment groups was recorded daily …”

Section: Methodsmentioning

confidence: 99%

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Design of a Novel Lysine Isopeptide 1018KI11 with Potent Antimicrobial Activity as a Safe and Stable Food Preservative Candidate

Wang,

Yang,

Dong

et al. 2024

J. Agric. Food Chem.

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Antimicrobial peptides are potent food additive candidates, but most of them are sensitive to proteases, which limits their application. Therefore, we substituted arginine for lysine and introduced a lysine isopeptide bond to peptide IDR-1018 in order to improve its enzymatic stability. Subsequently, the protease stability and antimicrobial/antibiofilm activity of the novel peptides (1018K2−1018KI11) were investigated. The data revealed that the antienzymatic potential of 1018KI11 to bromelain and papain increased by 2−8 folds and 16 folds, respectively. The minimum inhibitory concentration (MIC) of 1018KI11 against methicillinresistant Staphylococcus aureus (MRSA) ATCC43300 and Escherichia coli (E. coli) ATCC25922 was reduced 2-fold compared to 1018K11. Mechanism exploration suggested that 1018KI11 was more effective than 1018K11 in disrupting the cell barrier and damaging genomic DNA. Additionally, 1018KI11 at certain concentration conditions (2−64 μg/mL) reduced biofilm development of MRSA ATCC43300 by 4.9−85.9%. These data indicated that novel peptide 1018KI11 is a potential food preservative candidate.

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Section: Methodsmentioning

confidence: 99%

“…Finally, all samples were immediately stored at 4 °C for 5 days, and then the number of bacteria in the different treatment groups was recorded daily. 27 2.12. In Vivo Toxicity of 1018KI11.…”

Section: Application Of 1018ki11 In Chicken Breastmentioning

confidence: 99%

Design of a Novel Lysine Isopeptide 1018KI11 with Potent Antimicrobial Activity as a Safe and Stable Food Preservative Candidate

Wang,

Yang,

Dong

et al. 2024

J. Agric. Food Chem.

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“…48 Yang et al reported on the antimicrobial activity of a set of nonapeptides designed based on the sequence RXRXRXRXL-NH by introducing different ratios (W : I = 1 : 3, 2 : 2, and 3 : 1) of aromatic residues (Trp, W) and branched-chain residues (Ile, I) in the X position. 49 They found that the presence of Trp at the 4th and 6th loci of the nonapeptide sequence facilitated the formation of a β-pleated sheet with a certain turn conformation, indicating that these two positions determine structural flexibility (Fig. 4a and b).…”

Section: Interaction With Bacterial Membranes – Design Rulesmentioning

confidence: 97%

Engineering the interaction of short antimicrobial peptides with bacterial barriers

Montis,

Marelli,

Valle

et al. 2024

Mol. Syst. Des. Eng.

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“…Antimicrobial peptides (AMPs) have drawn a lot of attention as a treatment for germs that are resistant to numerous drugs. In the majority of multicellular organisms, antimicrobial peptides serve as the initial innate immune system defense [25,26]. Antimicrobial peptides serve as a crucial first line of defense for the body's immune system.…”

Section: Introductionmentioning

confidence: 99%

Anti-Proteolytic Peptide R7I Protects the Intestinal Barrier and Alleviates Fatty Acid Malabsorption in Salmonella typhimurium-Infected Mice

Su,

Sun,

Gao

et al. 2023

IJMS

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With a wide range of hosts, environmental adaptation, and antibiotic resistance, Salmonella typhimurium is one of the most common causes of food poisoning in the world. Infection with Salmonella typhimurium not only results in intestinal inflammation but also damages the intestinal barrier and interferes with the host’s ability to absorb nutrients. It is imperative to find alternatives to antibiotics for eradicating bacteria, reducing intestinal damage, and reestablishing nutrient absorption, especially given that antibiotics are currently prohibited. This research aims to understand the protective role of anti-proteolytic peptide R7I on the gut in the setting of Salmonella typhimurium infection and its impact on nutritional absorption, maybe offering an alternative to antibiotics for bacterial killing. The findings demonstrated that R7I reduced the production of inflammatory factors, including IL-6, TNF-α, and L-1β in the jejunum and decreased the expression of genes like TLR4 and NF-κB in the jejunum (p < 0.05). R7I enhanced antioxidant capacity and preserved the antioxidant/pro-oxidant balance in the jejunum (p < 0.05). R7I also normalized intestinal shape and restored tight junction protein expression. Fatty acid binding protein 2 (FABP2) and fatty acid transport protein 4 (FATP4) expression in the jejunum was restored by R7I. In addition, serum-free fatty acids and lipid metabolites were significantly higher in the R7I group than in the control group (p < 0.05). Overall, the anti-enzyme peptide R7I maintained the healthy state of the intestine and alleviated the abnormal fatty acid absorption caused by bacterial infection.

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Characterization of simplified nonapeptides with broad-spectrum antimicrobial activities as potential food preservatives, and their antibacterial mechanism

Abstract: The nonapeptides 3IW (RIRIRIRWL-NH2) and W2IW (RWRIRIRWL-NH2) based on a β-pleated sheet template have potent broad-spectrum antimicrobial effects via membrane disruption and ROS accumulation, and show favorable preservative effects in chicken meat.

Cited by 10 publications

References 66 publications

Design of a Novel Lysine Isopeptide 1018KI11 with Potent Antimicrobial Activity as a Safe and Stable Food Preservative Candidate

Design of a Novel Lysine Isopeptide 1018KI11 with Potent Antimicrobial Activity as a Safe and Stable Food Preservative Candidate

Engineering the interaction of short antimicrobial peptides with bacterial barriers

Anti-Proteolytic Peptide R7I Protects the Intestinal Barrier and Alleviates Fatty Acid Malabsorption in Salmonella typhimurium-Infected Mice

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