Action Mechanism of Peptide Variants with Antimicrobial, Anti-biofilm, or Anti-inflammatory Effects

A special issue of Antibiotics (ISSN 2079-6382).

Deadline for manuscript submissions: 31 July 2024 | Viewed by 5230

Special Issue Editor


E-Mail Website
Guest Editor
National Institute of Ecology, Seocheon, Korea
Interests: antimicrobial mechanism; antibiotic drug discovery; biochemical and genetic study of plant defense system; redox regulation; Genetically Modified Organism (GMO, LMO)
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Developing antimicrobial peptides (AMPs) is essential for serving effective and non-toxic antibiotic agents against various natural infection factors such as bacteria, fungi, and multidrug-resistant cell strains. Other functions of AMPs, such as anti-inflammatory and anti-biofilm activity, are also exciting topics. However, many AMPs are in the clinical phase for several infections, but have not entered the market as approved drugs. Therefore, there is an urgent need to discover, develop, and characterize novel natural antimicrobial agents and their functions. This Special Issue aims to bring together current views, new insights, and cutting-edge research on the characterization of functions and mechanisms of various AMPs. These contain AMPs from every species, including plants, yeasts, and mammals, and range from prokaryotes to eukaryotes.

I look forward to your contribution.

Dr. Jung Ro Lee
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. 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
  • cytotoxicity
  • action mode
  • anti-inflammation
  • anti-biofilm

Published Papers (3 papers)

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

Research

12 pages, 2995 KiB  
Article
Anti-Biofilm Effects of Rationally Designed Peptides against Planktonic Cells and Pre-Formed Biofilm of Pseudomonas aeruginosa
by Young-Min Kim, Hyosuk Son, Seong-Cheol Park, Jong-Kook Lee, Mi-Kyeong Jang and Jung Ro Lee
Antibiotics 2023, 12(2), 349; https://doi.org/10.3390/antibiotics12020349 - 8 Feb 2023
Cited by 7 | Viewed by 1835
Abstract
Biofilms are resistant to antibiotics and are a major source of persistent and recurring infections by clinically important pathogens. Drugs used for biofilm-associated infections are limited because biofilm-embedded or biofilm-matrix bacteria are difficult to kill or eradiate. Therefore, many researchers are developing new [...] Read more.
Biofilms are resistant to antibiotics and are a major source of persistent and recurring infections by clinically important pathogens. Drugs used for biofilm-associated infections are limited because biofilm-embedded or biofilm-matrix bacteria are difficult to kill or eradiate. Therefore, many researchers are developing new and effective antibiofilm agents. Among them, antimicrobial peptides have an attractive interest in the development of antibiofilm agents. The present study evaluated the effects of 10 synthetic peptides on growth inhibition, inhibition of biofilm formation, and biofilm elimination in drug-resistant Pseudomonas aeruginosa. The planktonic cell growth and biofilm formation were dose-dependently inhibited by most of the peptides. WIK-14 eliminated preformed biofilm masses by removing carbohydrates, extracellular nucleic acids, proteins, and lipids constituting extracellular polymeric substances. The results demonstrated that WIK-14 and WIKE-14 peptides might provide novel therapeutic drugs to overcome multidrug resistance in biofilm-associated infections. Full article
Show Figures

Figure 1

12 pages, 6709 KiB  
Article
Antifungal and Anti-Inflammatory Activities of PS1-2 Peptide against Fluconazole-Resistant Candida albicans
by Jong-Kook Lee, Soyoung Park, Young-Min Kim, Taeuk Guk, Jong Kwon Choi, Jin-Young Kim, Min-Young Lee, Mi-Kyeong Jang and Seong-Cheol Park
Antibiotics 2022, 11(12), 1779; https://doi.org/10.3390/antibiotics11121779 - 8 Dec 2022
Cited by 1 | Viewed by 1326
Abstract
Clinically, fungal pneumonia rarely occurs in adults, and invasive fungal infections can cause substantial morbidity, and mortality due to sepsis and septic shock. In the present study, we have designed peptides that exhibit potent antifungal activities against fluconazole-resistant Candida albicans in physiological monovalent, [...] Read more.
Clinically, fungal pneumonia rarely occurs in adults, and invasive fungal infections can cause substantial morbidity, and mortality due to sepsis and septic shock. In the present study, we have designed peptides that exhibit potent antifungal activities against fluconazole-resistant Candida albicans in physiological monovalent, and divalent ionic buffers, with minimal fungicidal concentrations ranging from 16 to 32 µM. None of these tested peptides resulted in the development of drug resistance similar to fluconazole. Among them, the PS1-2 peptide did not induce stimulation of macrophages by C. albicans, and it exerted antifungal and anti-inflammatory effects against C. albicans-induced intratracheal infection, in an acute lung injury mouse model. PS1-2 is likely a novel therapeutic agent for the control, and prevention of drug-resistant C. albicans infection, and our findings may be useful for designing antimicrobial peptides to combat fungal infection. Full article
Show Figures

Figure 1

14 pages, 3609 KiB  
Article
Potent Anti-Inflammatory Effects of a Helix-to-Helix Peptide against Pseudomonas aeruginosa Endotoxin-Mediated Sepsis
by Hyosuk Son, Seong-Cheol Park, Young-Min Kim, Jong-Kook Lee, Soyoung Park, Taeuk Guk, A-Mi Yoon, Hye Song Lim, Mi-Kyeong Jang and Jung Ro Lee
Antibiotics 2022, 11(11), 1675; https://doi.org/10.3390/antibiotics11111675 - 21 Nov 2022
Cited by 5 | Viewed by 1660
Abstract
Although considerable scientific research data is available for sepsis and cytokine storm syndrome, there is a need to develop new treatments or drugs for sepsis management. Antimicrobial peptides (AMPs) possess anti-bacterial and anti-inflammatory activity, neutralizing toxins such as lipopolysaccharides (LPS, endotoxin). Most AMPs [...] Read more.
Although considerable scientific research data is available for sepsis and cytokine storm syndrome, there is a need to develop new treatments or drugs for sepsis management. Antimicrobial peptides (AMPs) possess anti-bacterial and anti-inflammatory activity, neutralizing toxins such as lipopolysaccharides (LPS, endotoxin). Most AMPs have been designed as a substitute for conventional antibiotics, which kill drug-resistant pathogens. The present study aimed to determine the anti-inflammatory potential of 10 designed XIW (X: lysine, arginine, or glutamic acid) α-helical peptides in macrophages and a mouse model in the presence of LPS. Among them, WIKE-14, a peptide with a helix-to-helix structure, having the 12th amino acid substituted with glutamic acid, suppressed pro-inflammatory cytokines in RAW 264.7 macrophages. This reaction was mediated by the inhibition of the binding between LPS and macrophages. In addition, the WIKE-14 peptide exhibited a potent anti-inflammatory activity in mice ears and lungs inflamed using LPS. Thus, our results may provide useful insights for the development of anti-sepsis agents via the sequence and structure information of the WIKE-14 peptide. Full article
Show Figures

Figure 1

Back to TopTop