Advances in Marine Antimicrobial Peptides

A special issue of Marine Drugs (ISSN 1660-3397).

Deadline for manuscript submissions: closed (31 December 2021) | Viewed by 14708

Special Issue Editor


E-Mail Website
Guest Editor
Marine Research Station, Institute of Cellular and Organismic Biology, Academia Sinica, Jiaushi, Ilan, Taiwan
Interests: antimicrobial peptide; epinecidin-1; piscidin; anti-tumor peptide; sepsis; marine biotechnology; transgenic technology

Special Issue Information

Dear Colleagues,                

Antibiotics are the drugs of choice for treatment of and prophylaxis against pathogenic infections. The discovery and clinical application of antibiotics have greatly reduced the rates of mortality and morbidity throughout the world. However, the widespread and improper overuse of these molecules has caused the rise of drug-resistant pathogens. The evolution of resistant microbes has markedly reduced the overall potency of antibiotics. The recurring development of drug-resistant pathogens is a growing concern, which may create a post-antibiotic era that would compromise many of the medical advancements made in the past decades. It has been estimated that approximately 30 million individuals will die due to drug-resistant pathogens by the middle of this century. Hence, researchers have prioritized the discovery and development of new antibiotics or antibiotic alternatives for clinical applications. In this regard, marine antimicrobial peptides (AMPs) are thought to be one of the most promising classes of molecules for the development of alternatives to existing antibiotics. Marine AMPs are active molecules from nature’s arsenal that possess significant biocidal activity against a variety of non-resistant and resistant pathogens. Marine organisms produce many AMPs that may have unexpected applications and functions, which make them good candidates for use in promoting human, animal, and plant health or in the pursuit of basic scientific knowledge. The mechanisms governing the function of marine AMPs, such as those regarding evolution, endocrinology, immunology, etc., are largely unknown.

For this Special Issue, we aim to collect original research articles about AMPs from marine organisms, such as fish, shellfish, algae, abalone, coral, etc. Detailed research reports on the anti-bacterial, anti-viral, anti-sepsis, anti-tumor, anti-parasite, and other activities of marine AMPs are welcome for submission. The manuscripts may study AMPs from either a basic science (molecular mechanisms) or an applied science (translation science) perspective; both aquatic science and medical science submissions are welcome. Important findings of novel biological functions of marine AMPs will be especially exciting to the readers and the editor. If you use marine AMPs in any research context, we would greatly appreciate receiving your related submission. We hope the research results on marine AMPs published in this Special Issue will help to stimulate a new era for the improvement of human life and knowledge.


Dr. Jyh-Yih Chen
Guest Editor

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. Marine Drugs 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

  • Marine antimicrobial peptide
  • Drug-resistant
  • Antimicrobial activity
  • Anti-tumor
  • Anti-parasite
  • Aquatic research
  • Medical research

Published Papers (4 papers)

Order results
Result details
Select all
Export citation of selected articles as:

Research

14 pages, 2531 KiB  
Article
Investigations on the Wound Healing Potential of Tilapia Piscidin (TP)2-5 and TP2-6
by Chia-Wen Liu, Chu-Yi Hsieh and Jyh-Yih Chen
Mar. Drugs 2022, 20(3), 205; https://0-doi-org.brum.beds.ac.uk/10.3390/md20030205 - 10 Mar 2022
Cited by 3 | Viewed by 2459
Abstract
Wound healing is a highly orchestrated process involving many cell types, such as keratinocytes, fibroblasts and endothelial cells. This study aimed to evaluate the potential application of synthetic peptides derived from tilapia piscidin (TP)2, TP2-5 and TP2-6 in skin wound healing. The treatment [...] Read more.
Wound healing is a highly orchestrated process involving many cell types, such as keratinocytes, fibroblasts and endothelial cells. This study aimed to evaluate the potential application of synthetic peptides derived from tilapia piscidin (TP)2, TP2-5 and TP2-6 in skin wound healing. The treatment of HaCaT keratinocytes with TP2-5 and TP2-6 did not cause cytotoxicity, but did enhance cell proliferation and migration, which could be attributed to the activation of epidermal growth factor receptor signaling. In CCD-966SK fibroblasts, although TP2-5 (31.25 μg/mL) and TP2-6 (125 μg/mL) showed cytotoxic effects, we observed the significant promotion of cell proliferation and migration at low concentrations. In addition, collagen I, collagen III, and keratinocyte growth factor were upregulated by the peptides. We further found that TP2-5 and TP2-6 showed pro-angiogenic properties, including the enhancement of human umbilical vein endothelial cell (HUVEC) migration and the promotion of neovascularization. In a murine model, wounds treated topically with TP2-5 and TP2-6 were reduced by day 2 post-injury and healed significantly faster than untreated wounds. Taken together, these findings demonstrate that both TP2-5 and TP2-6 have multifaceted effects when used as topical agents for accelerating wound healing. Full article
(This article belongs to the Special Issue Advances in Marine Antimicrobial Peptides)
Show Figures

Figure 1

11 pages, 2282 KiB  
Article
Marine Antimicrobial Peptide TP4 Exerts Anticancer Effects on Human Synovial Sarcoma Cells via Calcium Overload, Reactive Oxygen Species Production and Mitochondrial Hyperpolarization
by Bor-Chyuan Su, Giun-Yi Hung, Yun-Chieh Tu, Wei-Chen Yeh, Meng-Chieh Lin and Jyh-Yih Chen
Mar. Drugs 2021, 19(2), 93; https://0-doi-org.brum.beds.ac.uk/10.3390/md19020093 - 05 Feb 2021
Cited by 6 | Viewed by 2424
Abstract
Synovial sarcoma is a rare but aggressive soft-tissue sarcoma associated with translocation t(X;18). Metastasis occurs in approximately 50% of all patients, and curative outcomes are difficult to achieve in this group. Since the efficacies of current therapeutic approaches for metastatic synovial sarcoma remain [...] Read more.
Synovial sarcoma is a rare but aggressive soft-tissue sarcoma associated with translocation t(X;18). Metastasis occurs in approximately 50% of all patients, and curative outcomes are difficult to achieve in this group. Since the efficacies of current therapeutic approaches for metastatic synovial sarcoma remain limited, new therapeutic agents are urgently needed. Tilapia piscidin 4 (TP4), a marine antimicrobial peptide, is known to exhibit multiple biological functions, including anti-bacterial, wound-healing, immunomodulatory, and anticancer activities. In the present study, we assessed the anticancer activity of TP4 in human synovial sarcoma cells and determined the underlying mechanisms. We first demonstrated that TP4 can induce necrotic cell death in human synovial sarcoma AsKa-SS and SW982 cells lines. In addition, we saw that TP4 initiates reactive oxygen species (ROS) production and downregulates antioxidant proteins, such as uncoupling protein-2, superoxide dismutase (SOD)-1, and SOD-2. Moreover, TP4-induced mitochondrial hyperpolarization is followed by elevation of mitochondrial ROS. Calcium overload is also triggered by TP4, and cell death can be attenuated by a necrosis inhibitor, ROS scavenger or calcium chelator. In our experiments, TP4 displayed strong anticancer activity in human synovial sarcoma cells by disrupting oxidative status, promoting mitochondrial hyperpolarization and causing calcium overload. Full article
(This article belongs to the Special Issue Advances in Marine Antimicrobial Peptides)
Show Figures

Figure 1

9 pages, 1144 KiB  
Article
A Pilot Safety Assessment for Recombinant Epinephelus lanceolatus Piscidin Yeast Powder as a Drug Food Additive after Subacute and Subchronic Administration to SD Rats
by Bor-Chyuan Su, Chao-Chin Li, Chia-Wen Liu and Jyh-Yih Chen
Mar. Drugs 2020, 18(12), 586; https://0-doi-org.brum.beds.ac.uk/10.3390/md18120586 - 24 Nov 2020
Viewed by 5874
Abstract
Recombinant Epinephelus lanceolatus piscidin (RELP) was previously shown to improve growth performance and immune response when used as a feed additive for Gallus gallus domesticus. However, the long-term toxicity of RELP has not be thoroughly investigated. In the present study, we evaluated [...] Read more.
Recombinant Epinephelus lanceolatus piscidin (RELP) was previously shown to improve growth performance and immune response when used as a feed additive for Gallus gallus domesticus. However, the long-term toxicity of RELP has not be thoroughly investigated. In the present study, we evaluated the subacute and subchronic oral toxicities of RELP in SD rats by hematological, biochemical, and histopathological analyses. To determine subacute and subchronic toxicities, male and female rats were fed with RELP 1000 mg/kg bodyweight/day for 28 and 90 days, respectively. Bodyweight and food intake were unchanged by RELP treatment over the course of the studies. After exposure, samples of blood, heart, lung, liver, and kidney were collected and analyzed. Results demonstrated that RELP exposure did not cause any observable hematological, biochemical, or histological abnormalities in SD rats. Thus, RELP may be a safe feed additive for use in agriculture and aquaculture. Full article
(This article belongs to the Special Issue Advances in Marine Antimicrobial Peptides)
Show Figures

Figure 1

14 pages, 2518 KiB  
Article
Antimicrobial Peptide TP4 Targets Mitochondrial Adenine Nucleotide Translocator 2
by Bor-Chyuan Su, Yi-Chung Liu, Chen-Hung Ting, Ping-Chiang Lyu and Jyh-Yih Chen
Mar. Drugs 2020, 18(8), 417; https://0-doi-org.brum.beds.ac.uk/10.3390/md18080417 - 09 Aug 2020
Cited by 11 | Viewed by 3085
Abstract
Tilapia piscidin (TP) 4 is an antimicrobial peptide derived from Nile tilapia (Oreochromis niloticus), which shows broad-spectrum antibacterial activity and excellent cancer-killing ability in vitro and in vivo. Like many other antimicrobial peptides, TP4 treatment causes mitochondrial toxicity in cancer cells. [...] Read more.
Tilapia piscidin (TP) 4 is an antimicrobial peptide derived from Nile tilapia (Oreochromis niloticus), which shows broad-spectrum antibacterial activity and excellent cancer-killing ability in vitro and in vivo. Like many other antimicrobial peptides, TP4 treatment causes mitochondrial toxicity in cancer cells. However, the molecular mechanisms underlying TP4 targeting of mitochondria remain unclear. In this study, we used a pull-down assay on A549 cell lysates combined with LC-MS/MS to discover that TP4 targets adenine nucleotide translocator (ANT) 2, a protein essential for adenine nucleotide exchange across the inner membrane. We further showed that TP4 accumulates in mitochondria and colocalizes with ANT2. Moreover, molecular docking studies showed that the interaction requires Phe1, Ile2, His3, His4, Ser11, Lys14, His17, Arg21, Arg24 and Arg25 residues in TP4 and key residues within the cavity of ANT2. These findings suggest a mechanism by which TP4 may induce mitochondrial dysfunction to disrupt cellular energy metabolism. Full article
(This article belongs to the Special Issue Advances in Marine Antimicrobial Peptides)
Show Figures

Figure 1

Back to TopTop