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Antibiotics
Special Issues
Antimicrobial Peptides (AMPs): Structure, Target, Spatiotemporal Relationship, and Druggability
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Antimicrobial Peptides (AMPs): Structure, Target, Spatiotemporal Relationship, and Druggability

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

Deadline for manuscript submissions: 30 June 2024 | Viewed by 3901

Special Issue Editors

Prof. Dr. Jianhua Wang

E-Mail Website
Guest Editor
1. Key Laboratory of Feed Biotechnology, Chinese Ministry of Agriculture and Rural Affairs, Beijing 100081, China
2. Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing 100081, China
Interests: antimicrobial peptides; drug resistance; expression; pathogenology; druggability; bacteria; Pichia pastoris; Staphycococus aures; MRSA; E. coli
Dr. Milena Mechkarska

E-Mail Website
Guest Editor
Department of Life Sciences, Faculty of Science and Technology, The University of the West Indies (The UWI), St. Augustine Campus, St. Augustine, Trinidad and Tobago
Interests: antimicrobial peptides; bioactive host-defence peptides; immunomodulators; venoms; novel therapeutics; drug development; host-pathogen interactions and host response to infections; multi-drug resistant

Special Issue Information

Dear Colleagues,

Antibiotic resistance has been expanding and spreading around the world and has become a threat to global public health. Antimicrobial peptides are a class of small molecular peptides produced by organisms to resist the invasion of exogenous pathogenic microorganisms. Compared with traditional antibiotics, antimicrobial peptides demonstrate a broad antibacterial spectrum and good thermal stability. Antimicrobial peptides also have different mechanisms to decrease the emergence of resistance. The use of antimicrobial peptides is a promising strategy to combat antibiotic resistance.

Exploring the structure–activity relationship of antimicrobial peptides to maximize their activity and reduce their cytotoxicity is the hotspot of antimicrobial peptides. In addition, understanding the mechanism of action of antimicrobial peptides and their responses to bacteria and host cells will allow their widespread use in clinical practice.

This Special Issue welcomes state-of-the-art research submissions focused on the following areas (mainly but not limited to):

  1. Structure disclosure and reveal of new AMPs during the early period of finding;
  2. Target finding and characteristic confirmation of new AMPs in pathogens and animals;
  3. Spatiotemporal relationship between/among AMPs, pathogens and host animals to pave their basis of pharmacology;
  4. Druggability of AMPs to reveal their pharmacological potentials in pathogens in vitro and in animal models and pre-clinical studies in vivo;
  5. Evaluation of potential resistance mechanisms towards AMPs in a variety of pathogens.

Prof. Dr. Jianhua Wang
Dr. Milena Mechkarska
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 (AMPs)
  • structure
  • target
  • spatiotemporal relationship
  • pharmacology
  • druggability

Published Papers (3 papers)

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Research

17 pages, 2778 KiB  
Article
ApoE Mimetic Peptide COG1410 Kills Mycobacterium smegmatis via Directly Interfering ClpC’s ATPase Activity
by Chun Wang, Yun-Yao Ren, Li-Mei Han, Peng-Cheng Yi, Wei-Xiao Wang, Cai-Yun Zhang, Xiu-Zhen Chen, Ming-Zhe Chi, Apeng Wang, Wei Chen and Chun-Mei Hu
Antibiotics 2024, 13(3), 278; https://doi.org/10.3390/antibiotics13030278 - 19 Mar 2024
Viewed by 793
Abstract
Antimicrobial peptides (AMPs) hold promise as alternatives to combat bacterial infections, addressing the urgent global threat of antibiotic resistance. COG1410, a synthetic peptide derived from apolipoprotein E, has exhibited potent antimicrobial properties against various bacterial strains, including Mycobacterium smegmatis. However, our study [...] Read more.
Antimicrobial peptides (AMPs) hold promise as alternatives to combat bacterial infections, addressing the urgent global threat of antibiotic resistance. COG1410, a synthetic peptide derived from apolipoprotein E, has exhibited potent antimicrobial properties against various bacterial strains, including Mycobacterium smegmatis. However, our study reveals a previously unknown resistance mechanism developed by M. smegmatis against COG1410 involving ClpC. Upon subjecting M. smegmatis to serial passages in the presence of sub-MIC COG1410, resistance emerged. The comparative genomic analysis identified a point mutation in ClpC (S437P), situated within its middle domain, which led to high resistance to COG1410 without compromising bacterial fitness. Complementation of ClpC in mutant restored bacterial sensitivity. In-depth analyses, including transcriptomic profiling and in vitro assays, uncovered that COG1410 interferes with ClpC at both transcriptional and functional levels. COG1410 not only stimulated the ATPase activity of ClpC but also enhanced the proteolytic activity of Clp protease. SPR analysis confirmed that COG1410 directly binds with ClpC. Surprisingly, the identified S437P mutation did not impact their binding affinity. This study sheds light on a unique resistance mechanism against AMPs in mycobacteria, highlighting the pivotal role of ClpC in this process. Unraveling the interplay between COG1410 and ClpC enriches our understanding of AMP-bacterial interactions, offering potential insights for developing innovative strategies to combat antibiotic resistance. Full article
(This article belongs to the Special Issue Antimicrobial Peptides (AMPs): Structure, Target, Spatiotemporal Relationship, and Druggability)
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11 pages, 19305 KiB  
Article
The Effect of Antimicrobial Peptide (PA-13) on Escherichia coli Carrying Antibiotic-Resistant Genes Isolated from Boar Semen
by Krittika Keeratikunakorn, Ratchaneewan Aunpad, Natharin Ngamwongsatit and Kampon Kaeoket
Antibiotics 2024, 13(2), 138; https://doi.org/10.3390/antibiotics13020138 - 31 Jan 2024
Viewed by 1188
Abstract
A major global public health concern is antimicrobial resistance (AMR). Antimicrobial peptides (AMPs) are a potentially appropriate replacement for conventional antibiotics. The purpose of this research was to investigate the potential of the antimicrobial peptide PA-13, a synthetic AMP with 13 amino acids, [...] Read more.
A major global public health concern is antimicrobial resistance (AMR). Antimicrobial peptides (AMPs) are a potentially appropriate replacement for conventional antibiotics. The purpose of this research was to investigate the potential of the antimicrobial peptide PA-13, a synthetic AMP with 13 amino acids, to inhibit E. coli isolated from boar semen expressing antibiotic-resistant genes, as well as to determine the mechanism of action of this antimicrobial peptide on the bacterial membrane. The effectiveness of the bacterial inhibitory activity of PA-13 was tested at different concentrations by two fold serial dilutions in the range 0.488–500 µg/mL using the MIC and MBC methods. The impact of PA-13 on the bacterial membrane was examined at different concentrations of 0×, 0.5×, 1×, 2× and 4× of MIC using DNA leakage assay and electron microscopy. The PA-13 antibacterial activity result exhibited the same MIC and MBC values at a concentration of 15.625 µg/mL. When comparing DNA leakage at different MIC values, the results revealed that the maximum amount of DNA concentration was found two and three hours after incubation. For the results of SEM and TEM, the bacterial membrane disruption of this E. coli was found in the PA-13-treated group when compared with the negative control. In conclusion, synthetic PA-13 with its antibacterial properties is an alternative antimicrobial peptide to antibiotics in the pig industry. Full article
(This article belongs to the Special Issue Antimicrobial Peptides (AMPs): Structure, Target, Spatiotemporal Relationship, and Druggability)
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21 pages, 4133 KiB  
Article
Site Mutation Improves the Expression and Antimicrobial Properties of Fungal Defense
by Ya Hao, Da Teng, Ruoyu Mao, Na Yang and Jianhua Wang
Antibiotics 2023, 12(8), 1283; https://doi.org/10.3390/antibiotics12081283 - 3 Aug 2023
Cited by 6 | Viewed by 1122
Abstract
Although antimicrobial peptides (AMPs) have highly desirable intrinsic characteristics in their commercial product development as new antimicrobials, the limitations of AMPs from experimental to scale development include the low oral bioavailability, and high production costs due to inadequate in vitro/in vivo gene expression- [...] Read more.
Although antimicrobial peptides (AMPs) have highly desirable intrinsic characteristics in their commercial product development as new antimicrobials, the limitations of AMPs from experimental to scale development include the low oral bioavailability, and high production costs due to inadequate in vitro/in vivo gene expression- and low scale. Plectasin has good bactericidal activity against Staphylococcus and Streptococcus, and the selective bactericidal activity greatly reduces the damage to the micro-ecosystem when applied in vivo. However, its expression level was relatively low (748.63 mg/L). In view of these situations, this study will optimize and modify the structure of Plectasin, hoping to obtain candidates with high expression, no/low toxicity, and maintain desirable antibacterial activity. Through sequence alignment, Plectasin was used as a template to introduce the degenerate bases, and the screening library was constructed. After three different levels of screening, the candidate sequence PN7 was obtained, and its total protein yield in the supernatant was 5.53 g/L, with the highest value so far for the variants or constructs from the same ancestor source. PN7 had strong activity against several species of Gram-positive bacteria (MIC value range 1~16 μg/mL). It was relatively stable in various conditions in vitro; in addition, the peptide showed no toxicity to mice for 1 week after intraperitoneal injection. Meanwhile, PN7 kills Staphylococcus aureus ATCC 43300 with a mode of a quicker (>99% S. aureus was killed within 2 h, whereas vancomycin at 2× MIC was 8 h.) and longer PAE period. The findings indicate that PN7 may be a novel promising antimicrobial agent, and this study also provides a model or an example for the design, modification, or reconstruction of novel AMPs and their derivatives. Full article
(This article belongs to the Special Issue Antimicrobial Peptides (AMPs): Structure, Target, Spatiotemporal Relationship, and Druggability)
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