Synergistic activity and immunomodulatory potential of levofloxacin and Synoeca‐MP peptide against multi-resistant strains of Klebsiella pneumoniae

Farias, Jade Ormondes de; Ferreira, Arthur Corrêa Resende; Kostopoulos, Alessandra Godoi Cardoso; Rezende, Taia Maria Berto; Dias, Simoni Campos

doi:10.1016/j.micpath.2022.105403

Cited by 5 publications

(10 citation statements)

References 43 publications

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“…These are cyclic Pps, classified according to the number of disulfide bridges made between the six cysteine residues preserved during evolution (α-and β-defensin and the macrocyclic structure θ-defensin). As with cathelicidins, defensins are also synthesized as inactive precursors, requiring proteolytic cleavage for activation [26].…”

Section: General Properties / Characteristics Of Antimicrobial Peptidesmentioning

confidence: 99%

Properties / Characteristics of Antimicrobial Peptides

Varga¹

2022

J Med Healthcare

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Antimicrobial peptides (AMPs) are natural antibiotics, synthesized by ribosomes, with an effect on the natural immunity of animal organisms. AMPs differ in composition [sequence and type of amino acids (AAs)] and structure, which contribute to rapid lysis and have a varied spectrum of antimicrobial activity. AMPs are: peptides (Pps) with alpha-helix structure (i.e., cecropins, magainins, mellitin, etc.); cyclic Pps and ring with several cysteine residues (i.e., defensins, protegrins, etc.); Pps rich in one or another AA (i.e., proline arginine-rich PR39, histidine, glycine, etc.). Most AMPs are characterized by hydrophobic and cationic properties, adopt an amphipathic structure (alpha-helix, spiral beta or alpha-helix / spiral beta), which is essential for antimicrobial activity. AMPs have the potential for therapeutic use in medicine. One of the major concerns of life sciences research is finding new ways to enhance the body’s defense against pathogens. One way is to produce drugs based on AMPs. The AMPs are a class of small Pps that have the ability to destroy pathogens of microbial and viral origin. The mechanisms of action are known only partially and for a small number of AMPs, and the toxic action of AMPs is generally considered to be based on the induction by these molecules in the outer membrane of the pathogen of aqueous pores that facilitate nonspecific ion transfer, which ultimately leads to lysis of the target cell.

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Section: General Properties / Characteristics Of Antimicrobial Peptidesmentioning

confidence: 99%

Properties / Characteristics of Antimicrobial Peptides

Varga¹

2022

J Med Healthcare

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“…Furthermore, AMPs can affect the maintenance of the integrity of the intestinal barrier by stimulating mucus synthesis and promoting the production of tight junction proteins and the repair of the endothelium ( 9 , 10 ). Interestingly, accumulating evidence shows the synergistic effects between AMPs or between AMPs and antibiotics, and these combinations can significantly reduce bacterial resistance ( 11 – 13 ). Owing to these favorable characteristics with infrequent drug resistance, broad-spectrum antimicrobial activities, rapid killing effects, and high capacity for synergies, AMPs have been considered attractive candidates for alternative antibiotics.…”

Section: Introductionmentioning

confidence: 99%

A novel antimicrobial peptide screened by a Bacillus subtilis expression system, derived from Larimichthys crocea Ferritin H, exerting bactericidal and parasiticidal activities

et al. 2023

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Antimicrobial peptides (AMPs) may be the most promising substitute for antibiotics due to their effective antimicrobial activities and multiple function mechanisms against pathogenic microorganisms. In this study, a novel AMP containing 51 amino acids, named Lc1687, was screened from the large yellow croaker (Larimichthys crocea) via a B. subtilis system. Bioinformatics and circular dichroism (CD) analyses showed that Lc1687 is a novel anionic amphiphilic α-helical peptide, which was derived from the C-terminal of a Ferritin heavy subunit. The recombinant Lc1687 (named rLc1687) purified from Escherichia coli exhibited strong activities against Gram-positive (Gram+) bacterium Staphylococcus aureus, Gram-negative (Gram-) bacteria Vibrio vulnificus, V. parahaemolyticus, and Scuticociliatida. Scanning electron microscope (SEM) and transmission electron microscopy (TEM) revealed the possible function mechanisms of this peptide, which is to target and disrupt the bacterial cell membranes, including pore-forming, loss of fimbriae, and cytoplasm overflow, whereas gel retardation assay revealed that peptide Lc1687 cannot bind bacterial DNA. The peptide stability analysis showed that rLc1687 acts as a stable antimicrobial agent against Gram+ and Gram- bacteria at temperatures ranging from 25 to 100°C, pH 3-12, and UV radiation time ranging from 15 to 60 min. A hemolytic activity assay confirmed that this peptide may serve as a potential source for clinical medicine development. Taken together, Lc1687 is a novel AMP as it is a firstly confirmed Ferritin fragment with antimicrobial activity. It is also a promising agent for the development of peptide-based antibacterial and anti-parasitic therapy.

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“…[ 18 ] Synoeca‐MP has already been tested in synergy with other drugs such as chlorhexidine and levofloxacin, which increased its activity against Pseudomonas aeruginosa and Klebsiella pneumoniae , respectively. [ 19,20 ] Regarding immune cytokines, synoeca‐MP has been shown to stimulate the production of pro‐inflammatory cytokines, such as TNF‐α and nitric oxide. [ 20 ] Due to its low hemolytic and cytotoxic activities, several biotechnological applications have been used to obtain efficient and cost‐effective approaches for the recombinant production and purification of this peptide.…”

Section: Introductionmentioning

confidence: 99%

“…[ 19,20 ] Regarding immune cytokines, synoeca‐MP has been shown to stimulate the production of pro‐inflammatory cytokines, such as TNF‐α and nitric oxide. [ 20 ] Due to its low hemolytic and cytotoxic activities, several biotechnological applications have been used to obtain efficient and cost‐effective approaches for the recombinant production and purification of this peptide. [ 21 ]…”

Section: Introductionmentioning

confidence: 99%

“…[19,20] Regarding immune cytokines, synoeca-MP has been shown to stimulate the production of proinflammatory cytokines, such as TNF-α and nitric oxide. [20] Due to its low hemolytic and cytotoxic activities, several biotechnological applications have been used to obtain efficient and cost-effective approaches for the recombinant production and purification of this peptide. [21] In this work, we report the first structural characterization of synoeca-MP in SDS micellar solutions using a combination of biophysical techniques such as NMR, CD and molecular dynamics.…”

Section: Introductionmentioning

confidence: 99%

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Synoeca‐MP: New insights into its mechanism of action by using NMR and molecular dynamics simulations approach

et al. 2022

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Synoeca-MP is a 14-residue amidated peptide, belongs to the mastoparan family and it is found in the venom of the wasp Synoeca surinama and has antibacterial and antifungal activity. The low cytotoxicity of the peptide also makes it an excellent candidate for drug development. To better understand its selectivity and interaction with the membrane, the peptide behavior in membrane-like environments was studied here and the peptide structure in SDS micelles was determined by NMR spectroscopy. The behavior of the peptide in hydrophobic media and in different pH ranges was studied by CD spectroscopy. The incorporation of residues into the anionic micelles was studied by hydrogen-deuterium exchange. The peptide stability and insertion in the micelles was studied by molecular dynamics simulations. Synoeca-MP, bound to SDS micelles, exhibits a partial α-helix conformation, with the first five residues and the last two unfolded. H/D exchange showed that the peptide has a slow exchange rate. After 164 h, four residues had not yet completed H/D substitution, suggesting parallel alignment of the peptide with the micelle, mainly due to the hydrophobic interface. This may indicate a carpet interaction model of the peptide with micelles. The molecular simulation study of peptide showed that the peptide consists of a well-folded alpha-helix core and unfolded extremities, which are responsible for the nature of the peptide interaction. The biophysical analyses can improve

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Synergistic activity and immunomodulatory potential of levofloxacin and Synoeca‐MP peptide against multi-resistant strains of Klebsiella pneumoniae

Cited by 5 publications

References 43 publications

Properties / Characteristics of Antimicrobial Peptides

Properties / Characteristics of Antimicrobial Peptides

A novel antimicrobial peptide screened by a Bacillus subtilis expression system, derived from Larimichthys crocea Ferritin H, exerting bactericidal and parasiticidal activities

Synoeca‐MP: New insights into its mechanism of action by using NMR and molecular dynamics simulations approach

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