Design, Characterization, and Antimicrobial Activity of a Novel Antimicrobial Peptide Derived from Bovine Lactophoricin

Kim, Jisun; Joeng, Ji-Ho; Kim, Yongae

doi:10.4014/jmb.1609.09004

Cited by 19 publications

(5 citation statements)

References 34 publications

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“…From the AFM imaging process, we suggest that SRP-2 could interact and disrupt bacterial membranes to perform its bactericidal activity. Previous studies have indicated that the interactions of an AMP with membrane components should result in conformational changes of the peptide 44 – 46 ; therefore, we applied CD spectroscopic measurements to examine the secondary structure changes of SRP-2 in membrane-mimicking environments. Moreover, 50% TFE has been used as one of the standard procedures for the induction of secondary structures of peptides in CD spectroscopy 47 – 50 .…”

Section: Resultsmentioning

confidence: 99%

An engineered arginine-rich α-helical antimicrobial peptide exhibits broad-spectrum bactericidal activity against pathogenic bacteria and reduces bacterial infections in mice

Yang

Chen

Peng

et al. 2018

Sci Rep

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The increase in the prevalence of antibiotic-resistant bacteria has become a major public health concern. Antimicrobial peptides (AMPs) are emerging as promising candidates addressing this issue. In this study, we designed several AMPs by increasing α-helical contents and positive charges and optimizing hydrophobicity and amphipathicity in the Sushi 1 peptide from horseshoe crabs. A neural network–based bioinformatic prediction tool was used for the first stage evaluations of peptide properties. Among the peptides designed, Sushi-replacement peptide (SRP)-2, an arginine-rich and highly α-helical peptide, showed broad-spectrum bactericidal activity against both Gram-positive and Gram-negative bacteria, including methicillin-resistant Staphylococcus aureus and multidrug-resistant Acinetobacter baumannii; nevertheless, it showed little hemolytic and cytotoxic activity against mammalian cells. Atomic force microscopy results indicated that SRP-2 should interact directly with cell membrane components, resulting in bacterial cell death. SRP-2 also neutralized LPS-induced macrophage activation. Moreover, in an intraperitoneal multidrug-resistant A. baumannii infection mouse model, SRP-2 successfully reduced the bacterial number in ascitic fluid and tumor necrosis factor-α production. Our study findings demonstrate that bioinformatic calculations can be powerful tools to help design potent AMPs and that arginine is superior to lysine for providing positive charges for AMPs to exhibit better bactericidal activity and selectivity against bacterial cells.

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Section: Resultsmentioning

confidence: 99%

An engineered arginine-rich α-helical antimicrobial peptide exhibits broad-spectrum bactericidal activity against pathogenic bacteria and reduces bacterial infections in mice

Yang

Chen

Peng

et al. 2018

Sci Rep

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“…All the sequences had a disordered conformation in 1X PBS, while the original peptide and the four active derivatives (35409-1, -2, -4 and -13) had negative signals at~208 and 222 nm in SDS micelles (Figure 1), such signals being characteristic of an α-helix pattern [53]. AMPs' usual pattern consists of a disordered tendency in solution and the adoption of structural tendencies defined in a membrane or solvent environment simulating it, such as SDS [51,52,70]. A helix structure is the commonest one for AMPs, suggested here for all peptides acting against E. coli; for example, an α-helix structure is involved in 18.8% of the 41.5% of peptides having a known structure in the APD3 database (http://aps.unmc.edu/AP/statistic/statistic_structure.php).…”

Section: Discussionmentioning

confidence: 99%

Shorter Antibacterial Peptide Having High Selectivity for E. coli Membranes and Low Potential for Inducing Resistance

et al. 2020

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Antimicrobial peptides (AMPs) have been recognised as a significant therapeutic option for mitigating resistant microbial infections. It has been found recently that Plasmodium falciparum-derived, 20 residue long, peptide 35409 had antibacterial and haemolytic activity, making it an AMP having reduced selectivity, and suggesting that it should be studied more extensively for obtaining new AMPs having activity solely targeting the bacterial membrane. Peptide 35409 was thus used as template for producing short synthetic peptides (<20 residues long) and evaluating their biological activity and relevant physicochemical characteristics for therapeutic use. Four of the sixteen short peptides evaluated here had activity against E. coli without any associated haemolytic effects. The 35409-1 derivative (17 residues long) had the best therapeutic characteristics as it had high selectivity for bacterial cells, stability in the presence of human sera, activity against E. coli multiresistant clinical isolates and was shorter than the original sequence. It had a powerful membranolytic effect and low potential for inducing resistance in bacteria. This peptide’s characteristics highlighted its potential as an alternative for combating infection caused by E. coli multiresistant bacteria and/or for designing new AMPs.

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“…As for the antibacterial activity, the interaction of AMPs with membrane components frequently correlates with antiviral effects, suggesting that the presence of a membrane could be one of the essential conditions in inducing the peptide conformation capable of inhibiting viral infection [57][58][59].…”

Section: Structural Characterization Of Rilk30 and Avp2mentioning

confidence: 99%

A Reliable Multifaceted Solution against Foodborne Viral Infections: The Case of RiLK1 Decapeptide

Galatola,

Agrillo,

Gogliettino

et al. 2024

Preprint

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Food-borne transmission is a recognized route for many viruses associated with gastrointestinal, hepatic or neurological diseases. Therefore, it is essential to identify new bioactive compounds with broad-spectrum antiviral activity is needed to exploit innovative solutions against these hazards. Lately, antimicrobial peptides (AMPs) have been recognized as promising antiviral agents. Indeed, while the antibacterial and antifungal effects of these molecules have been widely reported, their use as potential antiviral agents has not yet been fully investigated. Herein, the antiviral activity of previously identified or newly designed AMPs, was evaluated against the non-enveloped RNA viruses, Hepatitis A virus (HAV), and Murine Norovirus (MNV), a surrogate for human Norovirus. Moreover, specific assays were performed to recognize at which stage of the viral infection cycle the peptides could function. Results showed that almost all peptides displayed virucidal effects with about 90% of infectivity reduction on HAV or MNV. However, the decapeptide RiLK1 demonstrated, together with its antibacterial and antifungal properties, a notable reduction in viral infection for both HAV and MNV, possibly through direct interaction with viral particles or inhibition of the viral bonding to the cell receptors. Hence, RiLK1 could represent a versatile ‘antimicrobial agent effective against various foodborne pathogens including viruses, bacteria, and fungi.

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Design, Characterization, and Antimicrobial Activity of a Novel Antimicrobial Peptide Derived from Bovine Lactophoricin

Cited by 19 publications

References 34 publications

An engineered arginine-rich α-helical antimicrobial peptide exhibits broad-spectrum bactericidal activity against pathogenic bacteria and reduces bacterial infections in mice

An engineered arginine-rich α-helical antimicrobial peptide exhibits broad-spectrum bactericidal activity against pathogenic bacteria and reduces bacterial infections in mice

Shorter Antibacterial Peptide Having High Selectivity for E. coli Membranes and Low Potential for Inducing Resistance

A Reliable Multifaceted Solution against Foodborne Viral Infections: The Case of RiLK1 Decapeptide

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