Antimicrobial Peptides and How to Find Them

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

Deadline for manuscript submissions: closed (31 May 2022) | Viewed by 9059

Special Issue Editor


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Guest Editor
Faculty of Medicine, Ulm University, Ulm, Germany
Interests: bioactive peptides; synthesis; anti-infectives

Special Issue Information

Dear Colleagues,

The rise of multidrug-resistant microorganisms and the absence of new classical antibiotics have drawn attention to another class of antimicrobial molecules: antimicrobial peptides (AMPs). The term AMPs includes peptides acting against pathological bacteria, fungi (e.g., Candida and Aspergillus species), and new or mutated viruses such as ZIKA, Ebola, or SARS-CoV-2. In nature, AMPs are present in nearly all living organisms and act as a first or even exclusive line of defense against pathogenic germs, often also showing immunomodulatory functions.

For decades, researchers have managed to develop anti-infective medicines from such naturally occurring peptides. To date, more than ten peptide-based antibiotics are on the market (e.g., bacitracin, gramicidin, vancomycin, and others), and dozens are in clinical development.

The sources for AMPs are highly diverse and include mammals (e.g., cathelicidins, defensins), invertebrates, microorganisms, plants, and marine organisms. More than 3000 different AMPs have been annotated in the APD database (https://wangapd3.com). Today, bioinformatics tools are also employed in the design or amelioration (SAR analysis) of potent new AMPs using specific algorithms. In this Special Issue entitled “Antimicrobial Peptides: How to Find Them”, we invite publications on the search of novel antimicrobial peptides, based on either classical or modern methods, including predictions and the design of AMPs. Novel strategies focused on discovering AMPs against multidrug-resistant microorganisms are of particular interest in this Special Issue.

Dr. Ludger Stándker
Guest Editor

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Keywords

  • bioscreening
  • bioinformatics
  • antibacterial
  • antiviral
  • antifungal
  • multi-drug resistance
  • peptide chemistry

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Published Papers (3 papers)

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Research

13 pages, 3866 KiB  
Article
Optimized Chemical Extraction Methods of Antimicrobial Peptides from Roots and Leaves of Extremophilic Plants: Anthyllis sericea and Astragalus armatus Collected from the Tunisian Desert
by Raoua Ben Brahim, Hasna Ellouzi, Khaoula Fouzai, Nedra Asses, Mohammed Neffati, Jean Marc Sabatier, Philippe Bulet and Imed Regaya
Antibiotics 2022, 11(10), 1302; https://doi.org/10.3390/antibiotics11101302 - 24 Sep 2022
Cited by 6 | Viewed by 2802
Abstract
Extraction methods depend mainly on the chemical nature of the extracted molecule. For these reasons, the selection of the extraction medium is a vital part of obtaining these molecules. The extraction of antimicrobial peptides (AMPs) from extremophile plants is important because of its [...] Read more.
Extraction methods depend mainly on the chemical nature of the extracted molecule. For these reasons, the selection of the extraction medium is a vital part of obtaining these molecules. The extraction of antimicrobial peptides (AMPs) from extremophile plants is important because of its potential pharmaceutical applications. This work focused on the evaluation of several solvents for the extraction of AMPs from the following two extremophile plants: Astragalus armatus and Anthyllis sericea from southern Tunisia. In order to identify the most efficient solvents and extraction solutions, we used sulfuric acid, dichloromethane, phosphate buffer, acetic acid and sodium acetate, and we tested them on leaves and roots of both the studied plants. The extracts obtained using sulfuric acid, dichloromethane and phosphate buffer extraction did not show any antimicrobial activity, whereas the acetic acid and sodium acetate extracts led to growth inhibition of some of the tested bacterial strains. The extracts of leaves and roots of An. sericea and As. armatus obtained by acetic acid and sodium acetate were proven to be active against Gram-positive bacteria and Gram-negative bacteria. Therefore, the most appropriate solvents to use for antimicrobial peptide extraction from both plants are acetic acid and sodium acetate. Full article
(This article belongs to the Special Issue Antimicrobial Peptides and How to Find Them)
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20 pages, 2752 KiB  
Article
Performance of Novel Antimicrobial Protein Bg_9562 and In Silico Predictions on Its Properties with Reference to Its Antimicrobial Efficiency against Rhizoctonia solani
by Pranathi Karnati, Rekha Gonuguntala, Kalyani M. Barbadikar, Divya Mishra, Gopaljee Jha, Vellaisamy Prakasham, Priyanka Chilumula, Hajira Shaik, Maruthi Pesari, Raman Meenakshi Sundaram and Kannan Chinnaswami
Antibiotics 2022, 11(3), 363; https://doi.org/10.3390/antibiotics11030363 - 8 Mar 2022
Cited by 3 | Viewed by 3204
Abstract
Bg_9562 is a potential broad-spectrum antifungal effector protein derived from the bacteria Burkholderia gladioli strain NGJ1 and is effective against Rhizoctonia solani, the causal agent of sheath blight in rice. In the present study, in vitro antifungal assays showed that Bg_9562 was [...] Read more.
Bg_9562 is a potential broad-spectrum antifungal effector protein derived from the bacteria Burkholderia gladioli strain NGJ1 and is effective against Rhizoctonia solani, the causal agent of sheath blight in rice. In the present study, in vitro antifungal assays showed that Bg_9562 was efficient at 35 °C and 45 °C and ineffective either at high acidic pH (3.0) or alkaline pH (9.5) conditions. Compatibility studies between the native bioagents Trichoderma asperellum TAIK1 and Bacillus subtilis BIK3 indicated that Bg_9562 was compatible with the bioagents. A field study using foliar spray of the Bg_9562 protein indicated the need of formulating the protein before its application. In silico analysis predicted that Bg_9562 possess 111 amino acid residues (46 hydrophobic residues, 12 positive and 8 negative residues) with the high aliphatic index of 89.92, attributing to its thermostability with a half-life of 30 h. Bg_9562 (C491H813N137O166S5) possessed a protein binding potential of 1.27 kcal/mol with a better possibility of interacting and perturbing the membrane, the main target for antimicrobial proteins. The secondary structure revealed the predominance of random coils in its structure, and the best 3D model of Bg_9562 was predicted using an ab initio method with Robetta and AlphaFold 2. The predicted binding ligands were nucleic acids and zinc with confidence scores of 0.07 and 0.05, respectively. The N-terminal region (1–14 residues) and C-terminal region (101 to 111) of Bg_9562 residues were predicted to be disordered regions. Stability and binding properties of the protein from the above studies would help to encapsulate Bg_9562 using a suitable carrier to maintain efficiency and improve delivery against Rhizoctonia solani in the most challenging rice ecosphere. Full article
(This article belongs to the Special Issue Antimicrobial Peptides and How to Find Them)
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13 pages, 2546 KiB  
Article
The Silkworm as a Source of Natural Antimicrobial Preparations: Efficacy on Various Bacterial Strains
by Maristella Mastore, Silvia Quadroni, Sara Caramella and Maurizio Francesco Brivio
Antibiotics 2021, 10(11), 1339; https://doi.org/10.3390/antibiotics10111339 - 2 Nov 2021
Cited by 8 | Viewed by 2400
Abstract
The global spread of multi-resistant pathogens responsible for infections, which cannot be treated with existing drugs such as antibiotics, is of particular concern. Antibiotics are becoming increasingly ineffective and drug resistance is leading to more difficult-to-treat infections; therefore, new bioactive compounds with antimicrobial [...] Read more.
The global spread of multi-resistant pathogens responsible for infections, which cannot be treated with existing drugs such as antibiotics, is of particular concern. Antibiotics are becoming increasingly ineffective and drug resistance is leading to more difficult-to-treat infections; therefore, new bioactive compounds with antimicrobial activity are needed and new alternative sources should be found. Antimicrobial peptides (AMPs) are synthesized by processes typical of the innate immune system and are present in almost all organisms. Insects are extremely resistant to bacterial infections as they can produce a wide range of AMPs, providing an effective first line of defense. The AMPs produced by insects therefore represent a possible source of natural antimicrobial molecules. In this paper, the possibility of using plasma preparations from silkworm (Bombyx mori) larvae as a source of antimicrobials was evaluated. After simple purification steps, insect plasma was analyzed and tested on different Gram-positive and Gram-negative bacterial strains. The results obtained are encouraging as the assays on Escherichia coli and Enterobacter cloacae showed significant decrease in the growth of these Gram-negative bacteria. Similar results were obtained on Gram-positive bacteria, such as Micrococcus luteus and Bacillus subtilis, which showed strong susceptibility to the silkworm AMPs pool. In contrast, Staphylococcus aureus displayed high resistance to Bombyx mori plasma. Finally, the tested plasma formulations were assessed for possible storage not only at 4 °C, but also above room temperature. In conclusion, partially purified plasma from silkworm could be a promising source of AMPs which could be used in formulations for topical applications, without additional and expensive purification steps. Full article
(This article belongs to the Special Issue Antimicrobial Peptides and How to Find Them)
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