10th Anniversary of Antibiotics–Recent Advances in Antimicrobial Peptides

A special issue of Antibiotics (ISSN 2079-6382). This special issue belongs to the section "Antimicrobial Peptides".

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 36123

Special Issue Editors


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Guest Editor
Institute of Neurophysiopathology (INP), Aix-Marseille University, Faculté des sciences médicales et paramédicales, 27, Bd Jean Moulin, 13005 Marseille, France
Interests: antimicrobial peptides; antibacterial; antibiotics; structure-activity relationships; bacteriocins; drug design; peptide engineering
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Guest Editor
1. State Key Laboratory of Virology, College of Life Sciences, Shenzhen Research Institute, Wuhan University, Wuhan 430072, China
2. Key Laboratory of Fermentation Engineering (Ministry of Education), Hubei University of Technology, Wuhan 430068, China
Interests: animal venom peptides; scorpion toxins; ion channels; Mrgprs; antiviral peptides

Special Issue Information

Dear Colleagues,

The efficacy of antibiotics has been challenged in recent decades through the emergence of multidrug resistant bacteria and associated threat for humans and the other living organisms. Antibacterial peptides are part of the arsenal of host defense peptides that are present in a variety of more or less complex prokaryotic and eucaryotic life forms. Because of their particular antibacterial potential, they are currently emerging as candidate therapeutic drugs against both pathogenic Gram-positive and Gram-negative bacteria, including those resistant to conventional antibiotics. This Special Issue commemorating the 10th anniversary of the journal Antibiotics deals with all aspects of antibacterial peptides (from natural or non-natural sources), from their discovery to their evolution, structural/functional characterization, as well as their evaluation in clinical trials. Potential contributors from all countries are strongly encouraged to submit their works in this important field of scientific research.

The topic of this Special Issue is devoted to antimicrobial peptides (AMP). Some AMPs might be the next generation of antibiotics.

Dr. Jean-Marc Sabatier
Prof. Dr. Zhijian Cao
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Antibiotics is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Antimicrobial peptides
  • Antibacterial
  • Antibiotics
  • Structure–activity relationships
  • Bacteriocins
  • Drug design
  • Peptide engineering
  • Bacterial resistance

Published Papers (8 papers)

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Research

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19 pages, 2260 KiB  
Article
Creating Robust Antimicrobial Materials with Sticky Tyrocidines
by Wilma van Rensburg and Marina Rautenbach
Antibiotics 2022, 11(2), 174; https://doi.org/10.3390/antibiotics11020174 - 28 Jan 2022
Cited by 1 | Viewed by 2186
Abstract
Modified antimicrobial and antifouling materials and surfaces can be used to limit the propagation of microorganisms on various surfaces and minimise the occurrence of infection, transfer, and spoilage. Increased demand for ‘green’ solutions for material treatment has pushed the focus towards to naturally [...] Read more.
Modified antimicrobial and antifouling materials and surfaces can be used to limit the propagation of microorganisms on various surfaces and minimise the occurrence of infection, transfer, and spoilage. Increased demand for ‘green’ solutions for material treatment has pushed the focus towards to naturally produced antimicrobials. Tyrocidines, cyclo-decapeptides naturally produced by a soil bacterium Brevibacillus parabrevis, have a broad spectrum of activity against Gram-positive and Gram-negative bacteria, filamentous fungi, and yeasts. Continual losses in tyrocidine production highlighted the possible association of peptides to surfaces. It was found in this study that tyrocidines readily associates with many materials, with a selectivity towards polysaccharide-type materials, such as cellulose. Peptide-treated cellulose was found to remain active after exposure to a broad pH range, various temperatures, salt solutions, water washes, and organic solvents, with the sterilising activity only affected by 1% SDS and 70% acetonitrile. Furthermore, a comparison to other antimicrobial peptides showed the association between tyrocidines and cellulose to be unique in terms of antimicrobial activity. The robust association between the tyrocidines and various materials holds great promise in applications focused on preventing surface contamination and creating self-sterilising materials. Full article
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19 pages, 13361 KiB  
Article
Combinations of Peptide-Protein Extracts from Native Probiotics Suppress the Growth of Multidrug-Resistant Staphylococcus aureus and Citrobacter freundii via Membrane Perturbation and Ultrastructural Changes
by Gabriela N. Tenea, Evelyn Angamarca and Daniela Olmedo
Antibiotics 2022, 11(2), 154; https://doi.org/10.3390/antibiotics11020154 - 25 Jan 2022
Cited by 1 | Viewed by 2867
Abstract
The occurrence of multidrug-resistant pathogens in the food chain causes health problems in humans, thus, research for novel antimicrobials to combat their growth is of interest. This study evaluates the antimicrobial potential of several combinations of peptide-protein extracts (PCs) consisting of peptide extracts [...] Read more.
The occurrence of multidrug-resistant pathogens in the food chain causes health problems in humans, thus, research for novel antimicrobials to combat their growth is of interest. This study evaluates the antimicrobial potential of several combinations of peptide-protein extracts (PCs) consisting of peptide extracts from three native probiotic strains, Lactiplantibacillus plantarum UTNGt2, Lactococcus lactis UTNGt28, and L. plantarum UTNGt21A, alone or in combination with EDTA (ethylenediaminetetraacetic acid) against multidrug-resistant Staphylococcus aureus ATCC1026 and Citrobacter freundii UTNB3Sm1. Based on the antimicrobial assay, among the 19 tested PCs, two (PC11 and PC17) produced a greater zone of inhibition against both pathogens in vitro. Time-killing assays indicated the rapid death of S. aureus after exposure to PC11 and PC17, while C. freundii was rapidly inhibited by PC11 and PC1 (UTNGt2 only), suggesting that the inhibitory action is pathogen and dose-dependent of a particular molecule present in the extract. A marginal inhibitory effect was observed when the peptides were combined with EDTA. Transmission electron microscopy (TEM) revealed the structural membrane damage of both target strains upon interaction with individual peptide extracts. Different degrees of cell deformation, condensed cytoplasm, membrane blebbing, and ghost cell formation with visibly broken cell walls were observed in S. aureus. Likewise, the separation of the cytoplasmic membrane from the outer membrane, ghost cells, along with ovoid and deformed cells with undulated cell walls were observed for C. freundii. Furthermore, scanning electronic microscopy (SEM) analysis revealed different wrinkled and deformed cells covered by debris. A leakage of aromatic molecules was detected for both pathogens, indicating that PCs disrupted the cell wall integrity, inducing cell death. Given their inhibitory action and capacity to induce damage of the cytoplasmic membrane, the selected PCs may serve to slow bacterial growth in vitro; further research is required to prove their efficiency ex vitro to battle against food poisoning and subsequent human infection. Full article
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9 pages, 2046 KiB  
Article
The Small Metal-Binding Protein SmbP Simplifies the Recombinant Expression and Purification of the Antimicrobial Peptide LL-37
by David A. Perez-Perez, Teresa de J. Villanueva-Ramirez, Adriana E. Hernandez-Pedraza, Nestor G. Casillas-Vega, Patricia Gonzalez-Barranco and Xristo Zarate
Antibiotics 2021, 10(10), 1271; https://doi.org/10.3390/antibiotics10101271 - 19 Oct 2021
Cited by 5 | Viewed by 2566
Abstract
(1) Background: The cathelicidin peptide LL-37 is a prominent molecule with many biological activities, including antimicrobial. Due to its importance, here, we describe the production of LL-37 tagged with SmbP, a relatively new carrier protein that improves the production of recombinant proteins and [...] Read more.
(1) Background: The cathelicidin peptide LL-37 is a prominent molecule with many biological activities, including antimicrobial. Due to its importance, here, we describe the production of LL-37 tagged with SmbP, a relatively new carrier protein that improves the production of recombinant proteins and peptides in Escherichia coli. We present an alternative method for the rapid expression, purification, and antimicrobial evaluation of LL-37, that involves only one purification step. (2) Methods: A DNA construct of SmbP_LL-37 was transformed into E. coli BL21(DE3); after overnight expression, the protein was purified directly from the cell lysate using immobilized metal-affinity chromatography. SmbP_LL-37 was treated with Enterokinase to obtain the free LL-37 peptide. The antimicrobial activity of both SmbP_LL-37 and free LL-37 was determined using the colony forming unit assay method. (3) Results: SmbP_LL-37 was observed in the soluble fraction of the cell lysate; after purification with IMAC, protein gel electrophoresis, and analysis by ImageJ, it showed 90% purity. A total of 3.6 mg of SmbP_LL-37 was produced from one liter of cell culture. SmbP_LL-37 and free LL-37 both showed inhibition activity against Staphylococcus aureus and Escherichia coli. (4) Conclusions: The SmbP fusion protein is a valuable tool for producing biologically-active LL-37 peptide. The production method described here should be of interest for the expression and purification of additional cationic peptides, since it cuts the purification time considerably prior to determination of antimicrobial activity. Full article
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8 pages, 1337 KiB  
Article
Design, Synthesis and Antifungal Activity of Stapled Aurein1.2 Peptides
by Mengjun Zheng, Ruina Wang, Si Chen, Yan Zou, Lan Yan, Linjing Zhao and Xiang Li
Antibiotics 2021, 10(8), 956; https://doi.org/10.3390/antibiotics10080956 - 9 Aug 2021
Cited by 8 | Viewed by 2103
Abstract
Aurein1.2 is a 13-residue antimicrobial peptide secreted by the Australian tree frog Litoria aurea. In order to improve its stabilities, the helical contents and corresponding biological activities of Aurein1.2 (a series of stapled analogues) were synthesized, and their potential antifungal activities were [...] Read more.
Aurein1.2 is a 13-residue antimicrobial peptide secreted by the Australian tree frog Litoria aurea. In order to improve its stabilities, the helical contents and corresponding biological activities of Aurein1.2 (a series of stapled analogues) were synthesized, and their potential antifungal activities were evaluated. Not surprisingly, the stapled Aurein1.2 peptides showed higher proteolytic stability and helicity than the linear counterpart. The minimum inhibitory concentration (MIC) of ten stapled peptides against six strains of common pathogenic fungi was determined by the microscale broth dilution method recommended by CLSI. Of them, Sau-1, Sau-2, Sau-5, and Sau-9 exhibited better inhibitory effects on the fungi than the linear peptide. These stapled Aurein1.2 peptides may serve as the leading compounds for further optimization and antifungal therapy. Full article
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10 pages, 2505 KiB  
Article
Molecular Cloning and Functional Identification of the Antimicrobial Peptide Gene Ctri9594 from the Venom of the Scorpion Chaerilus tricostatus
by Dangui He, Zhijian Cao, Ruhong Zhang and Wenhua Li
Antibiotics 2021, 10(8), 896; https://doi.org/10.3390/antibiotics10080896 - 23 Jul 2021
Cited by 3 | Viewed by 1910
Abstract
Scorpion venom is a mixture of bioactive peptides, among which neurotoxins and antimicrobial peptides serve especially vital functions. Scorpion venom peptides in Buthidae species have been well described, but toxic peptides from non-Buthidae species have been under-investigated. Here, an antimicrobial peptide gene, Ctri9594, [...] Read more.
Scorpion venom is a mixture of bioactive peptides, among which neurotoxins and antimicrobial peptides serve especially vital functions. Scorpion venom peptides in Buthidae species have been well described, but toxic peptides from non-Buthidae species have been under-investigated. Here, an antimicrobial peptide gene, Ctri9594, was cloned and functionally identified from the venom of the scorpion Chaerilus tricostatus. The precursor nucleotide sequence of Ctri9594 is 199 nt in length, including a 43 nt 5′ UTR, 115 nt 3′ UTR and 210 nt ORF. The ORF encodes 69 amino acid residues, containing a 21 aa signal peptide, 14 aa mature peptide, 3 aa C-terminal posttranslational processing signal and 31 aa propeptide. Multiple sequence alignment and evolutionary analyses show that Ctri9594 is an antimicrobial peptide in scorpion venom. The mature peptide of Ctri9594 was chemically synthesized with a purity greater than 95% and a molecular mass of 1484.4 Da. Minimum inhibitory concentrations (MICs) indicate that the synthesized mature peptide of Ctri9594 has inhibitory activity against Gram-positive bacteria (Bacillus thuringensis, Bacillus subtilis, Staphylococcus aureus and Micrococcus luteus) but not Gram-negative bacteria (Escherichia coli and Pseudomonas aeruginosa) or a fungus (Candida albicans). The antimicrobial mechanism of Ctri9594 is inferred to be related to its amphiphilic α-helix structure. Full article
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13 pages, 2933 KiB  
Article
Super-Cationic Peptide Dendrimers—Synthesis and Evaluation as Antimicrobial Agents
by Estelle J. Ramchuran, Isabel Pérez-Guillén, Linda A. Bester, René Khan, Fernando Albericio, Miguel Viñas and Beatriz G. de la Torre
Antibiotics 2021, 10(6), 695; https://doi.org/10.3390/antibiotics10060695 - 10 Jun 2021
Cited by 5 | Viewed by 2648
Abstract
Microbial infections are a major public health concern. Antimicrobial peptides (AMPs) have been demonstrated to be a plausible alternative to the current arsenal of drugs that has become inefficient due to multidrug resistance. Herein we describe a new AMP family, namely the super-cationic [...] Read more.
Microbial infections are a major public health concern. Antimicrobial peptides (AMPs) have been demonstrated to be a plausible alternative to the current arsenal of drugs that has become inefficient due to multidrug resistance. Herein we describe a new AMP family, namely the super-cationic peptide dendrimers (SCPDs). Although all members of the series exert some antibacterial activity, we propose that special attention should be given to (KLK)2KLLKLL-NH2 (G1KLK-L2KL2), which shows selectivity for Gram-negative bacteria and virtually no cytotoxicity in HepG2 and HEK293. These results reinforce the validity of the SCPD family as a valuable class of AMP and support G1KLK-L2KL2 as a strong lead candidate for the future development of an antibacterial agent against Gram-negative bacteria. Full article
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Review

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15 pages, 1089 KiB  
Review
Antimicrobial Peptides: A Potent Alternative to Antibiotics
by Mariam Rima, Mohamad Rima, Ziad Fajloun, Jean-Marc Sabatier, Burkhard Bechinger and Thierry Naas
Antibiotics 2021, 10(9), 1095; https://doi.org/10.3390/antibiotics10091095 - 10 Sep 2021
Cited by 133 | Viewed by 13747
Abstract
Antimicrobial peptides constitute one of the most promising alternatives to antibiotics since they could be used to treat bacterial infections, especially those caused by multidrug-resistant pathogens. Many antimicrobial peptides, with various activity spectra and mechanisms of actions, have been described. This review focuses [...] Read more.
Antimicrobial peptides constitute one of the most promising alternatives to antibiotics since they could be used to treat bacterial infections, especially those caused by multidrug-resistant pathogens. Many antimicrobial peptides, with various activity spectra and mechanisms of actions, have been described. This review focuses on their use against ESKAPE bacteria, especially in biofilm treatments, their synergistic activity, and their application as prophylactic agents. Limitations and challenges restricting therapeutic applications are highlighted, and solutions for each challenge are evaluated to analyze whether antimicrobial peptides could replace antibiotics in the near future. Full article
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25 pages, 796 KiB  
Review
Beehive Products as Antibacterial Agents: A Review
by Rita Abou Nader, Rawan Mackieh, Rim Wehbe, Dany El Obeid, Jean Marc Sabatier and Ziad Fajloun
Antibiotics 2021, 10(6), 717; https://doi.org/10.3390/antibiotics10060717 - 15 Jun 2021
Cited by 25 | Viewed by 6633
Abstract
Honeybees are one of the most marvelous and economically beneficial insects. As pollinators, they play a vital role in every aspect of the ecosystem. Beehive products have been used for thousands of years in many cultures for the treatment of various diseases. Their [...] Read more.
Honeybees are one of the most marvelous and economically beneficial insects. As pollinators, they play a vital role in every aspect of the ecosystem. Beehive products have been used for thousands of years in many cultures for the treatment of various diseases. Their healing properties have been documented in many religious texts like the Noble Quran and the Holy Bible. Honey, bee venom, propolis, pollen and royal jelly all demonstrated a richness in their bioactive compounds which make them effective against a variety of bacterial strains. Furthermore, many studies showed that honey and bee venom work as powerful antibacterial agents against a wide range of bacteria including life-threatening bacteria. Several reports documented the biological activities of honeybee products but none of them emphasized on the antibacterial activity of all beehive products. Therefore, this review aims to highlight the antibacterial activity of honey, bee venom, propolis, pollen and royal jelly, that are produced by honeybees. Full article
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