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Antimicrobial Peptides and Their Synthetic Mimics
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Antimicrobial Peptides and Their Synthetic Mimics

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pharmacology".

Deadline for manuscript submissions: closed (28 April 2021) | Viewed by 10917

Special Issue Editors

Prof. Dr. Robert Bucki

E-Mail Website
Guest Editor
Department of Microbiological and Nanobiomedical Engineering, Medical University of Bialystok, Mickiewicza 2c, 15-222 Bialystok, Poland
Interests: biochemistry of lipids; antimicrobial peptides; plasma gelsolin; ceragenis; biopolymers; inflammation; cystic fibrosis; cell cytoskeleton; cell rheology
Special Issues, Collections and Topics in MDPI journals
Dr. Ewelina Piktel

E-Mail Website
Co-Guest Editor
Department of Medical Microbiology and Nanobiomedical Engineering, Medical University of Bialystok, Bialystok, Poland
Interests: antimicrobial peptides; nanotechnology; membrane-active compounds; drug resistance
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear colleagues, 

Since the discovery that antimicrobial peptides (AMPs) function as major host defense effectors, extensive research attention has been paid to this class of molecules as a likely source of potential therapeutics with a broad spectrum of antimicrobial, antitumor, and immunomodulatory activity. Some limitations to their potential as future drugs, most notably restricted bioavailability for systemic use, may be addressed by the development of peptidomimetics and other synthetic mimics that recapitulate key physicochemical properties responsible for AMP activity and membrane insertion. Additionally, the activity of AMPs, especially at sites of infection, is regulated by charge–driven interactions with various biopolymers, including extracellular DNA and F-actin. This Special Issue aims to provide a platform to accumulate knowledge on current strategies for the use and adaptation of AMPs as therapeutic agents against multidrug-resistant pathogens, various cancers, and as enhancers of the functions of the host's immune system.

Prof. Dr. Robert Bucki
Guest Editor
Dr. Ewelina Piktel
Co-Guest Editor

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Keywords

  • Antimicrobial peptide
  • Peptidomimetics
  • Structure–activity relationship
  • Bacterial resistance
  • Polyelectrolytes
  • Cancer
  • Host defence
  • Immunomodulatory activity
  • Membrane insertion

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Published Papers (3 papers)

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Research

43 pages, 2261 KiB  
Article
Polyphenylglyoxamide-Based Amphiphilic Small Molecular Peptidomimetics as Antibacterial Agents with Anti-Biofilm Activity
by Tsz Tin Yu, Rajesh Kuppusamy, Muhammad Yasir, Md. Musfizur Hassan, Manjulatha Sara, Junming Ho, Mark D. P. Willcox, David StC. Black and Naresh Kumar
Int. J. Mol. Sci. 2021, 22(14), 7344; https://doi.org/10.3390/ijms22147344 - 8 Jul 2021
Cited by 9 | Viewed by 3624
Abstract
The rapid emergence of drug-resistant bacteria is a major global health concern. Antimicrobial peptides (AMPs) and peptidomimetics have arisen as a new class of antibacterial agents in recent years in an attempt to overcome antibiotic resistance. A library of phenylglyoxamide-based small molecular peptidomimetics [...] Read more.
The rapid emergence of drug-resistant bacteria is a major global health concern. Antimicrobial peptides (AMPs) and peptidomimetics have arisen as a new class of antibacterial agents in recent years in an attempt to overcome antibiotic resistance. A library of phenylglyoxamide-based small molecular peptidomimetics was synthesised by incorporating an N-alkylsulfonyl hydrophobic group with varying alkyl chain lengths and a hydrophilic cationic group into a glyoxamide core appended to phenyl ring systems. The quaternary ammonium iodide salts 16d and 17c showed excellent minimum inhibitory concentration (MIC) of 4 and 8 μM (2.9 and 5.6 μg/mL) against Staphylococcus aureus, respectively, while the guanidinium hydrochloride salt 34a showed an MIC of 16 μM (8.5 μg/mL) against Escherichia coli. Additionally, the quaternary ammonium iodide salt 17c inhibited 70% S. aureus biofilm formation at 16 μM. It also disrupted 44% of pre-established S. aureus biofilms at 32 μM and 28% of pre-established E. coli biofilms 64 μM, respectively. A cytoplasmic membrane permeability study indicated that the synthesised peptidomimetics acted via disruption and depolarisation of membranes. Moreover, the quaternary ammonium iodide salts 16d and 17c were non-toxic against human cells at their therapeutic dosages against S. aureus. Full article
(This article belongs to the Special Issue Antimicrobial Peptides and Their Synthetic Mimics)
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15 pages, 4888 KiB  
Article
Antibacterial and Antibiofilm Activities of Novel Antimicrobial Peptides against Multidrug-Resistant Enterotoxigenic Escherichia Coli
by Kang-Chi Wu, Kuo-Feng Hua, Yu-Hsiang Yu, Yeong-Hsiang Cheng, Ting-Ting Cheng, Yao-Kuan Huang, Hui-Wen Chang and Wei-Jung Chen
Int. J. Mol. Sci. 2021, 22(8), 3926; https://doi.org/10.3390/ijms22083926 - 10 Apr 2021
Cited by 18 | Viewed by 3442
Abstract
Post-weaning diarrhea due to enterotoxigenic Escherichia coli (ETEC) is a common disease of piglets and causes great economic loss for the swine industry. Over the past few decades, decreasing effectiveness of conventional antibiotics has caused serious problems because of the growing emergence of [...] Read more.
Post-weaning diarrhea due to enterotoxigenic Escherichia coli (ETEC) is a common disease of piglets and causes great economic loss for the swine industry. Over the past few decades, decreasing effectiveness of conventional antibiotics has caused serious problems because of the growing emergence of multidrug-resistant (MDR) pathogens. Various studies have indicated that antimicrobial peptides (AMPs) have potential to serve as an alternative to antibiotics owing to rapid killing action and highly selective toxicity. Our previous studies have shown that AMP GW-Q4 and its derivatives possess effective antibacterial activities against the Gram-negative bacteria. Hence, in the current study, we evaluated the antibacterial efficacy of GW-Q4 and its derivatives against MDR ETEC and their minimal inhibition concentration (MIC) values were determined to be around 2~32 μg/mL. Among them, AMP Q4-15a-1 with the second lowest MIC (4 μg/mL) and the highest minimal hemolysis concentration (MHC, 256 μg/mL), thus showing the greatest selectivity (MHC/MIC = 64) was selected for further investigations. Moreover, Q4-15a-1 showed dose-dependent bactericidal activity against MDR ETEC in time–kill curve assays. According to the cellular localization and membrane integrity analyses using confocal microscopy, Q4-15a-1 can rapidly interact with the bacterial surface, disrupt the membrane and enter cytosol in less than 30 min. Minimum biofilm eradication concentration (MBEC) of Q4-15a-1 is 4× MIC (16 μg/mL), indicating that Q4-15a-1 is effective against MDR ETEC biofilm. Besides, we established an MDR ETEC infection model with intestinal porcine epithelial cell-1 (IPEC-1). In this infection model, 32 μg/mL Q4-15a-1 can completely inhibit ETEC adhesion onto IPEC-1. Overall, these results suggested that Q4-15a-1 may be a promising antibacterial candidate for treatment of weaned piglets infected by MDR ETEC. Full article
(This article belongs to the Special Issue Antimicrobial Peptides and Their Synthetic Mimics)
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17 pages, 2444 KiB  
Article
Insights into the Action Mechanism of the Antimicrobial Peptide Lasioglossin III
by Filomena Battista, Rosario Oliva, Pompea Del Vecchio, Roland Winter and Luigi Petraccone
Int. J. Mol. Sci. 2021, 22(6), 2857; https://doi.org/10.3390/ijms22062857 - 11 Mar 2021
Cited by 25 | Viewed by 3099
Abstract
Lasioglossin III (LL-III) is a cationic antimicrobial peptide derived from the venom of the eusocial bee Lasioglossum laticeps. LL-III is extremely toxic to both Gram-positive and Gram-negative bacteria, and it exhibits antifungal as well as antitumor activity. Moreover, it shows low hemolytic [...] Read more.
Lasioglossin III (LL-III) is a cationic antimicrobial peptide derived from the venom of the eusocial bee Lasioglossum laticeps. LL-III is extremely toxic to both Gram-positive and Gram-negative bacteria, and it exhibits antifungal as well as antitumor activity. Moreover, it shows low hemolytic activity, and it has almost no toxic effects on eukaryotic cells. However, the molecular basis of the LL-III mechanism of action is still unclear. In this study, we characterized by means of calorimetric (DSC) and spectroscopic (CD, fluorescence) techniques its interaction with liposomes composed of a mixture of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) and 1-palmitoyl-2-oleoyl-sn-glycero-3-rac-phosphoglycerol (POPG) lipids as a model of the negatively charged membrane of pathogens. For comparison, the interaction of LL-III with the uncharged POPC liposomes was also studied. Our data showed that LL-III preferentially interacted with anionic lipids in the POPC/POPG liposomes and induces the formation of lipid domains. Furthermore, the leakage experiments showed that the peptide could permeabilize the membrane. Interestingly, our DSC results showed that the peptide-membrane interaction occurs in a non-disruptive manner, indicating an intracellular targeting mode of action for this peptide. Consistent with this hypothesis, our gel-retardation assay experiments showed that LL-III could interact with plasmid DNA, suggesting a possible intracellular target. Full article
(This article belongs to the Special Issue Antimicrobial Peptides and Their Synthetic Mimics)
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