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Antibiotics
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Natural Peptides from Arthropods, Amphibians, and Reptiles to Combat Conventional...
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Natural Peptides from Arthropods, Amphibians, and Reptiles to Combat Conventional Antibiotic Resistance

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

Deadline for manuscript submissions: 31 December 2024 | Viewed by 9353

Special Issue Editors

Prof. Dr. Christopher Shaw

E-Mail Website
Guest Editor
School of Pharmacy, Queen's University Belfast, Belfast BT7 1NN, UK
Interests: natural peptide; mass spectrometry; antibiotic resistance; structure–activity relationship; membrane selectivity
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Tianbao Chen

E-Mail Website
Guest Editor
Natural Drug Discovery Group, School of Pharmacy, Queen’s University Belfast, Belfast BT7 1NN, UK
Interests: peptide science; antibiotic resistance; structure–activity relationship; drug design
Special Issues, Collections and Topics in MDPI journals
Dr. Lei Wang

E-Mail Website
Guest Editor
School of Pharmacy, Queen's University Belfast, Belfast BT7 1NN, UK
Interests: antimicrobial peptide; peptide modification; resistant strains; pharmacology

Special Issue Information

Dear Colleagues,

Infection with antibiotic-resistant pathogens poses an ever-increasing threat to public health. The discovery of novel antibiotic agents and approaches for tackling the antimicrobial resistance crisis has received increasing global attention. Arthropods, amphibians, and reptiles may play an increasingly important role in the prevention and treatment of antibiotic-resistant infections, as many recently discovered compounds from these natural sources are able to prevent the growth of, or indeed kill, antibiotic-resistant pathogens. While the intrinsic complexity of natural-product-based drug discovery necessitates highly integrated interdisciplinary approaches, there is currently an urgent need for new approaches to identifying and using natural compounds as antibiotic agents. Therefore, this Special Issue seeks research articles focused on our current knowledge of and recent advances in bioactive molecules from natural sources for the prevention and treatment of antibiotic-resistant infections. Articles might contribute in the following ways, but are not limited to: 

  • designing challenging and innovative approaches to the identification and development of novel peptides from natural sources against antibiotic-resistant pathogens;
  • elucidating the mode of action of natural peptides against antibiotic-resistant pathogens;
  • establishing new strategies for optimizing natural leads as antibiotic and/or drug candidates;
  • application of natural agents as adjuvants in the prevention and therapy of antibiotic-resistant infections;
  • applying novel modified biotechnological techniques in the production of natural antibiotics; and reviews of current issues and prospects in the treatment of antibiotic-resistant infections. 

Prof. Dr. Christopher Shaw
Prof. Tianbao Chen
Dr. Lei Wang
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 peptide
  • peptide modification
  • antibiotic resistance
  • structure–activity relationship
  • membrane selectivity
  • resistant strains

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Published Papers (3 papers)

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Research

22 pages, 11478 KiB  
Article
Kassporin-KS1: A Novel Pentadecapeptide from the Skin Secretion of Kassina senegalensis: Studies on the Structure-Activity Relationships of Site-Specific “Glycine-Lysine” Motif Insertions
by Yueyang Lu, Wanchen Zou, Lei Wang, Xinping Xi, Chengbang Ma, Xiaoling Chen, Tianbao Chen, Chris Shaw, Xu Zhang and Mei Zhou
Antibiotics 2022, 11(2), 243; https://doi.org/10.3390/antibiotics11020243 - 13 Feb 2022
Cited by 3 | Viewed by 2142
Abstract
Due to the abuse of traditional antibiotics and the continuous mutation of microbial resistance genes, microbial infections have become serious problems for human health. Therefore, novel antibacterial agents are urgently required, and amphibian antimicrobial peptides (AMP) are among the most interesting potential antibacterial [...] Read more.
Due to the abuse of traditional antibiotics and the continuous mutation of microbial resistance genes, microbial infections have become serious problems for human health. Therefore, novel antibacterial agents are urgently required, and amphibian antimicrobial peptides (AMP) are among the most interesting potential antibacterial leads. In this research, a novel peptide, named kassporin-KS1 (generically QUB-1641), with moderate antibacterial activity against Gram-positive bacteria, was discovered in the skin secretion of the Senegal running frog, Kassina senegalensis. Using site-specific sequence enrichment with a motif “glycine-lysine” that frequently occurs in ranid frog temporin peptides, a series of QUB-1641 analogues were synthesized, and effects on selected bioactivities were studied. The greatest activity enhancement was obtained when the “glycine-lysine” motif was located at the eighth and ninth position as in QUB-1570.QUB-1570 had a broader antibacterial spectrum than QUB-1641, and was eight-fold more potent. Moreover, QUB-1570 inhibited S. aureus biofilm most effectively, and significantly enhanced the viability of insect larvae infected with S. aureus. When the “glycine-lysine” motif of QUB-1570 was substituted to reduce the helix ratio and positive charge, the antibacterial activities of these synthetic analogues decreased. These data revealed that the “glycine-lysine” motif at positions 8 and 9 had the greatest enhancing effect on the antibacterial properties of QUB-1570 through increasing positive charge and helix content. This research may provide strategies for the site’s selective amino acid modification of some natural peptides to achieve the desired enhancement of activity. Full article
(This article belongs to the Special Issue Natural Peptides from Arthropods, Amphibians, and Reptiles to Combat Conventional Antibiotic Resistance)
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18 pages, 3383 KiB  
Article
Exploration of the Structure–Function Relationships of a Novel Frog Skin Secretion-Derived Bioactive Peptide, t-DPH1, through Use of Rational Design, Cationicity Enhancement and In Vitro Studies
by Haixin Qin, Hantian Fang, Xiaoling Chen, Lei Wang, Chengbang Ma, Xinping Xi, Tianbao Chen, Chris Shaw and Mei Zhou
Antibiotics 2021, 10(12), 1529; https://doi.org/10.3390/antibiotics10121529 - 14 Dec 2021
Cited by 8 | Viewed by 3070
Abstract
Amphibian skin-derived antimicrobial peptides (AMPs) have attracted increasing attention from scientists because of their excellent bioactivity and low drug resistance. In addition to being the alternative choice of antibiotics or anticancer agents, natural AMPs can also be modified as templates to optimise their [...] Read more.
Amphibian skin-derived antimicrobial peptides (AMPs) have attracted increasing attention from scientists because of their excellent bioactivity and low drug resistance. In addition to being the alternative choice of antibiotics or anticancer agents, natural AMPs can also be modified as templates to optimise their bioactivities further. Here, a novel dermaseptin peptide, t-DPH1, with extensive antimicrobial activity and antiproliferative activity, was isolated from the skin secretion of Phyllomedusa hypochondrialis through ‘shotgun’ cloning. A series of cationicity-enhanced analogues of t-DPH1 were designed to further improve its bioactivities and explore the charge threshold of enhancing the bioactivity of t-DPH1. The present data suggest that improving the net charge can enhance the bioactivities to some extent. However, when the charge exceeds a specific limit, the bioactivities decrease or remain the same. When the net charge achieves the limit, improving the hydrophobicity makes no sense to enhance bioactivity. For t-DPH1, the upper limit of the net charge was +7. All the designed cationicity-enhanced analogues produced no drug resistance in the Gram-negative bacterium, Escherichia coli. These findings provide creative insights into the role of natural drug discovery in providing templates for structural modification for activity enhancement. Full article
(This article belongs to the Special Issue Natural Peptides from Arthropods, Amphibians, and Reptiles to Combat Conventional Antibiotic Resistance)
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22 pages, 2831 KiB  
Article
Study on the Structure-Activity Relationship of an Antimicrobial Peptide, Brevinin-2GUb, from the Skin Secretion of Hylarana guentheri
by Yaxian Lin, Siyan Liu, Xinping Xi, Chengbang Ma, Lei Wang, Xiaoling Chen, Zhanzhong Shi, Tianbao Chen, Chris Shaw and Mei Zhou
Antibiotics 2021, 10(8), 895; https://doi.org/10.3390/antibiotics10080895 - 22 Jul 2021
Cited by 7 | Viewed by 3195
Abstract
Antimicrobial peptides (AMPs) are considered potential alternatives to antibiotics due to their advantages in solving antibiotic resistance. Brevinin-2GUb, which was extracted from the skin secretion of Hylarana guentheri, is a peptide with modest antimicrobial activity. Several analogues were designed to explore the [...] Read more.
Antimicrobial peptides (AMPs) are considered potential alternatives to antibiotics due to their advantages in solving antibiotic resistance. Brevinin-2GUb, which was extracted from the skin secretion of Hylarana guentheri, is a peptide with modest antimicrobial activity. Several analogues were designed to explore the structure–activity relationship and enhance its activity. In general, the Rana box is not an indispensable motif for the bioactivity of Brevinin-2GUb, and the first to the 19th amino acids at the N-terminal end are active fragments, such that shortening the peptide while maintaining its bioactivity is a promising strategy for the optimisation of peptides. Keeping a complete hydrophobic face and increasing the net charges are key factors for antimicrobial activity. With the increase of cationic charges, α-helical proportion, and amphipathicity, the activity of t-Brevinin-2GUb-6K (tB2U-6K), in combatting bacteria, drastically improved, especially against Gram-negative bacteria, and the peptide attained the capacity to kill clinical isolates and fungi as well, which made it possible to address some aspects of antibiotic resistance. Thus, peptide tB2U-6K, with potent antimicrobial activity against antibiotic-resistant bacteria, the capacity to inhibit the growth of biofilm, and low toxicity against normal cells, is of value to be further developed into an antimicrobial agent. Full article
(This article belongs to the Special Issue Natural Peptides from Arthropods, Amphibians, and Reptiles to Combat Conventional Antibiotic Resistance)
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