A novel milk-derived peptide effectively inhibits Staphylococcus aureus: Interferes with cell wall synthesis, peptidoglycan biosynthesis disruption reaction mechanism, and its application in real milk system

Li, Yufang; Yang, Kun; Wei, Guangqiang; Huang, Aixiang

doi:10.1016/j.foodcont.2022.109374

Cited by 13 publications

(15 citation statements)

References 30 publications

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“…BCp12, one of the most widely studied AMPs from milk protein, has been confirmed that can block bacterial PGN biosynthesis by down-regulating the expression level of bacterial proteins recently. 98 Moreover, as lipid II is an important component in PGN synthesis; 99 AMPs can bind to lipid II and hinder PGN synthesis, thereby triggering damage to the cell wall. 100 Mersacidin is a globular wool−sulfur antibiotic, 101 which targets lipid II and forms a complex with the sugar−phosphate headgroup, blocking the trans-glycosylation step in cell wall biosynthesis and ultimately acting as a bactericide.…”

Section: Nonmembrane Damaging Mechanisms 321 Inhibition Of Cell Walls...mentioning

confidence: 99%

“…In the framework of analyzing BCp12, it came to light that it is capable of suppressing nucleic acid synthesis by cutting the expression levels of deconjugating enzymes, DNA polymerase III holoenzymes, and DNA ligases during DNA replication in S. aureus. 98 Another example is buforin II, whose binding strength to cellular DNA and RNA is 20 times higher than that of magainin 2. This result reveals that buforin II binds to DNA and RNA after penetrating the cell membranes to impair normal cells' functioning.…”

Section: Inhibition Of Dna/rna and Polypeptide Synthesismentioning

confidence: 99%

“…It has been observed that BCp12 is capable of binding to the active sites of Mur ligases (MurC, MurD, MurE, MurF, and MurG), and play its antimicrobial activity. 98 4.3. Molecular Dynamics Simulation.…”

Section: Online Toolsmentioning

confidence: 99%

“…AMPs can cause damage to the cell wall by interfering with the biosynthesis of PGN. BCp12, one of the most widely studied AMPs from milk protein, has been confirmed that can block bacterial PGN biosynthesis by down-regulating the expression level of bacterial proteins recently . Moreover, as lipid II is an important component in PGN synthesis; AMPs can bind to lipid II and hinder PGN synthesis, thereby triggering damage to the cell wall .…”

Section: Activity Mechanisms Of Milk Protein Derived Ampsmentioning

confidence: 99%

“…For some AMPs, the primary mechanism act at the intracellular level is inhibiting the synthesis of DNA, RNA, and proteins. In the framework of analyzing BCp12, it came to light that it is capable of suppressing nucleic acid synthesis by cutting the expression levels of deconjugating enzymes, DNA polymerase III holoenzymes, and DNA ligases during DNA replication in S. aureus . Another example is buforin II, whose binding strength to cellular DNA and RNA is 20 times higher than that of magainin 2.…”

Section: Activity Mechanisms Of Milk Protein Derived Ampsmentioning

confidence: 99%

See 4 more Smart Citations

Recent Advances on Antimicrobial Peptides from Milk: Molecular Properties, Mechanisms, and Applications

Wang,

Xu,

Zeng

et al. 2023

J. Agric. Food Chem.

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Traditional antibiotics are facing a tremendous challenge due to increased antimicrobial resistance; hence, there is an urgent need to find novel antibiotic alternatives. Milk protein-derived antimicrobial peptides (AMPs) are currently attracting substantial attention considering that they showcase an extensive spectrum of antimicrobial activities, with slower development of antimicrobial resistance and safety of raw materials. This review summarizes the molecular properties, and activity mechanisms and highlights the applications and limitations of AMPs derived from milk proteins comprehensively. Also the analytical technologies, especially bioinformatics methodologies, applied in the process of screening, identification, and mechanism illustration of AMPs were underlined. This review will give some ideas for further research and broadening of the applications of milk protein-derived AMPs in the food field.

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Section: Nonmembrane Damaging Mechanisms 321 Inhibition Of Cell Walls...mentioning

confidence: 99%

Section: Inhibition Of Dna/rna and Polypeptide Synthesismentioning

confidence: 99%

Section: Online Toolsmentioning

confidence: 99%

Section: Activity Mechanisms Of Milk Protein Derived Ampsmentioning

confidence: 99%

Section: Activity Mechanisms Of Milk Protein Derived Ampsmentioning

confidence: 99%

See 3 more Smart Citations

Recent Advances on Antimicrobial Peptides from Milk: Molecular Properties, Mechanisms, and Applications

Wang,

Xu,

Zeng

et al. 2023

J. Agric. Food Chem.

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Antibacterial Peptides derived from Capra hircus Goat Milk Casein

Ningsih,

Habibie,

Haryadi

et al. 2024

ChemistrySelect

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Milk is a popular source of antimicrobial peptides (AMPs). Therefore, this study aimed to investigate antibacterial activity of fractions and peptides derived from casein hydrolysate. Casein protein was hydrolyzed using the trypsin enzyme and the hydrolyzate was fractionated with a strong cationic exchange (scx) cartridge at a pH 3–9 buffer. The results showed that the pH 5–8 fraction demonstrated antibacterial activity against Staphylococcus aureus and Escherichia coli. The pH 6 fraction had the greatest activity against S. aureus and E. coli, with inhibition zone of 8.00 and 2.00 mm, respectively. Peptides in the pH 6 fraction, namely YNVPQLEIVPK (P1), KENINELSK (P2), GLSPEVPNENLLR (P3), and YLGYLEQLLK (P4) were tested for the activity against S. aureus and E. coli. Based on the results, synthetic peptide P1, P2, P3, and P4 have activity against S. aureus and E. coli. Peptide P3 showed higher activity than others with an inhibition zone of 4.55 and 6.60 mm in S. aureus and E. coli, respectively. Peptide P4 showed an amphipathic structure and good physicochemical properties as a cell‐penetrating peptide. A strong interaction was also observed between peptide P4 and enzyme MurC with a binding affinity of −6.6 kcal/mol.

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FengycinA-M3 Inhibits Listeria monocytogenes by Binding to Penicillin-Binding Protein 2B Targets to Disrupt Cell Structure

Wang,

Tang,

Chen

et al. 2024

Probiotics & Antimicro. Prot.

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A novel milk-derived peptide effectively inhibits Staphylococcus aureus: Interferes with cell wall synthesis, peptidoglycan biosynthesis disruption reaction mechanism, and its application in real milk system

Cited by 13 publications

References 30 publications

Recent Advances on Antimicrobial Peptides from Milk: Molecular Properties, Mechanisms, and Applications

Recent Advances on Antimicrobial Peptides from Milk: Molecular Properties, Mechanisms, and Applications

Antibacterial Peptides derived from Capra hircus Goat Milk Casein

FengycinA-M3 Inhibits Listeria monocytogenes by Binding to Penicillin-Binding Protein 2B Targets to Disrupt Cell Structure

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