<i>In Vitro</i>
            and
            <i>In Vivo</i>
            Studies on the Antibacterial Activity and Safety of a New Antimicrobial Peptide Dermaseptin-AC

Chen, Jiajia; Hao, Doudou; Kai, Masahiro; Li, Xin; Ma, Chengbang; Xi, Xinping; Li, Lei; Wang, Lei; Liu, Jia; Wu, Qing

doi:10.1128/spectrum.01318-21

Cited by 9 publications

(4 citation statements)

References 40 publications

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“…Analysis of the antimicrobial activity of DS-THA was carried out by determining the minimal inhibitory concentration (MIC) for E. coli and B. subtilis. For both microorganisms MIC values of 1.6 µM were determined, being consistent with previous reported values (Chen et al, 2021;Dash and Bhattacharjya, 2021) and demonstrating the production of functional target (Supplementary Figure S7). After co-incubation of VHH, a single chain antibody fragment with binding affinity towards the fluorescent protein mCherry (Wang et al, 2021), the quantitative formation of VHH-mCherry heterodimers was observed by size exclusion chromatography (SEC) analysis (Supplementary Figure S8), proving the functional fold of VHH.…”

Section: Functional Characterizationsupporting

confidence: 90%

Numaswitch, a biochemical platform for the efficient production of disulfide-rich pepteins

Nguyen

Tieves²,

Neusius³

et al. 2023

Front. Drug Discov.

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The application of long-chained peptides (+30 aa) and relatively short proteins (<300 aa) has experienced an increasing interest in recent years. However, a reliable production platform is still missing since manufacturing is challenged by inherent problems such as mis-folding, aggregation, and low production yields. And neither chemical synthesis nor available recombinant approaches are effective and efficient. This in particular holds true for disulfide-rich targets where the correct isomer needs to be formed. With the technology Numaswitch, we have now developed a biochemical tool that circumvents existing limitations and serves as first production platform for pepteins, hard-to-be-produced peptides and proteins between 30 and 300 amino acids in length, including disulfide-rich candidates. Numaswitch is based on bifunctional Switchtag proteins that force the high-titer expression of pure inclusion bodies and simultaneously assist in the efficient refolding of pepteins into functional pepteins. Here, we demonstrate the successful application of the Numaswitch platform for disulfide-containing pepteins, such as an antimicrobial fusion peptide, a single-chain variable fragment (scFv), a camelid heavy chain antibody fragment (VHH) and the human epidermal growth factor.

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Section: Functional Characterizationsupporting

confidence: 90%

Numaswitch, a biochemical platform for the efficient production of disulfide-rich pepteins

Nguyen

Tieves²,

Neusius³

et al. 2023

Front. Drug Discov.

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“…Safety is the key factor that hinders the entry of AMPs into the clinical application [ 28 , 29 ]. Therefore, we measured the hemolytic rate of Pleu and its modified peptides.…”

Section: Resultsmentioning

confidence: 99%

Truncated Pleurocidin Derivative with High Pepsin Hydrolysis Resistance to Combat Multidrug-Resistant Pathogens

et al. 2022

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The global prevalence of antimicrobial resistance calls for the development of novel antimicrobial agents, particularly for these orally available drugs. Structural modifications of the natural antimicrobial peptides (AMPs) provide a straightforward approach to develop potent antimicrobial agents with high specificity and low toxicity. In this study, we truncated 11-amino-acids at the C-terminus of Pleurocidin, an AMP produced by Pleuronectes americanus, and obtained four peptide analogues termed GK-1, GK-2, GK-3 and GK-4. Minimum inhibitory concentration (MIC) tests showed that GK-1 obtained by direct truncation of Pleurocidin has no antibacterial activity, while GK-2, GK-3 and GK-4 show considerable antibacterial activity with Pleurocidin. Notably, GK-4 displays rapid bacteriostatic activity, great stability and low hemolysis, as well as enhanced hydrolytic resistance to pepsin treatment. Mechanistic studies showed that GK-4 induces membrane damage by interacting with bacterial membrane-specific components, dissipates bacterial membrane potential and promotes the generation of ROS. SEM and CD analysis further confirmed the ability of GK-4 to resist pepsin hydrolysis, which may be attributed to its stable helicity structure. Collectively, our findings reveal that GK-4 is a potential orally available candidate to treat infections caused by multidrug-resistant pathogens.

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“…As biologists have found, insects are able to produce an immensity of biologically active substances that can serve as a model for imitation or, more importantly, a new source for obtaining medicinal preparations. We can mention that these intentions have already given results, resulting in the introduction in medical practice of food supplements or entomological drugs with various properties [17].…”

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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In Vitro and In Vivo Studies on the Antibacterial Activity and Safety of a New Antimicrobial Peptide Dermaseptin-AC

Abstract: In this study, we discovered a new antimicrobial peptide, Dermaseptin-AC, and studied its in vitro and in vivo antimicrobial activity. These studies provide some data for finding new antimicrobial peptides for overcoming antimicrobial resistance.

Cited by 9 publications

References 40 publications

Numaswitch, a biochemical platform for the efficient production of disulfide-rich pepteins

Numaswitch, a biochemical platform for the efficient production of disulfide-rich pepteins

Truncated Pleurocidin Derivative with High Pepsin Hydrolysis Resistance to Combat Multidrug-Resistant Pathogens

Properties / Characteristics of Antimicrobial Peptides

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