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Antibiotics
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Antimicrobial Peptides from Natural Sources to Synthetic Optimization
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Antimicrobial Peptides from Natural Sources to Synthetic Optimization

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

Deadline for manuscript submissions: closed (31 March 2024) | Viewed by 11948

Special Issue Editors

Dr. Javier Eduardo García Castañeda

E-Mail Website
Guest Editor
Departamento de Farmacia, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá Carrera 45 No 26-85, Building 450, Bogotá 11321, Colombia
Interests: peptide synthesis; antimicrobial and anticancerigenic peptides; glycopeptides; organometallic peptides
Dr. Zuly Jenny Rivera-Monroy

E-Mail Website
Guest Editor
Departamento de Química, Facultad de Ciencias, Universidad Nacional de Colombia, Bogotá Carrera 45 No 26-85, Building 451, Bogotá 11321, Colombia
Interests: peptide synthesis; peptide therapeutic application; peptide analysis by HPLC and MS

Special Issue Information

Dear Colleagues,

Antimicrobial peptides (AMPs) are considered the main resource for the development of new therapeutic alternatives against antimicrobial infections. AMPs have been identified in plants and animals with very diverse primary and secondary structures, which give them physicochemical properties that are fundamental for their antimicrobial activity. It has been pointed out that AMPs have some deficiencies that limit their use as drugs, such as proteolytic susceptibility, easy and rapid elimination from the body, difficulty in crossing membranes, undesirable side effects, etc. Therefore, the identification of promising AMPs is the cornerstone in the development of drugs to mitigate the impact of antimicrobial infections, especially those caused by resistant strains. AMPs that have been identified and/or isolated from natural sources are the starting point for the design and development of new molecules with enhanced antimicrobial activity and in some cases these AMPs have been commercialized, increasing our therapeutic options. The design and optimization of peptide sequences involves different synthetic strategies such as: obtaining short linear sequences, dendrimers, cyclic peptides, dimeric peptides, tetrameric peptides, polymeric peptides, inclusion of non-natural amino acids, D-amino acids, organic molecules of non-peptide origin, etc. These modifications require the simultaneous use of methodologies such as solid phase and solution chemical synthesis, click chemistry, oxidation reactions, recombinant technology, etc. Although significant progress has been made in improving the antimicrobial activity of molecules, it is clear that much remains to be done as there is an urgent need for more therapeutic options to combat antimicrobial infections, which are now considered a global public health problem.

Dr. Javier Eduardo García Castañeda
Dr. Zuly Jenny Rivera-Monroy
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
  • mimetic peptides
  • defensins
  • antimicrobial proteins
  • dendrimeric peptides
  • peptide chemistry synthesis
  • recombinant peptide synthesis

Published Papers (7 papers)

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Research

18 pages, 3304 KiB  
Article
The Identification of a Novel Spider Toxin Peptide, Lycotoxin-Pa2a, with Antibacterial and Anti-Inflammatory Activities
by Min Kyoung Shin, In-Wook Hwang, Bo-Young Jang, Kyung-Bin Bu, Dong-Hee Han, Seung-Ho Lee, Jin Wook Oh, Jung Sun Yoo and Jung-Suk Sung
Antibiotics 2023, 12(12), 1708; https://doi.org/10.3390/antibiotics12121708 - 07 Dec 2023
Viewed by 1173
Abstract
With the increasing challenge of controlling infectious diseases due to the emergence of antibiotic-resistant strains, the importance of discovering new antimicrobial agents is rapidly increasing. Animal venoms contain a variety of functional peptides, making them a promising platform for pharmaceutical development. In this [...] Read more.
With the increasing challenge of controlling infectious diseases due to the emergence of antibiotic-resistant strains, the importance of discovering new antimicrobial agents is rapidly increasing. Animal venoms contain a variety of functional peptides, making them a promising platform for pharmaceutical development. In this study, a novel toxin peptide with antibacterial and anti-inflammatory activities was discovered from the spider venom gland transcriptome by implementing computational approaches. Lycotoxin-Pa2a (Lytx-Pa2a) showed homology to known-spider toxin, where functional prediction indicated the potential of both antibacterial and anti-inflammatory peptides without hemolytic activity. The colony-forming assay and minimum inhibitory concentration test showed that Lytx-Pa2a exhibited comparable or stronger antibacterial activity against pathogenic strains than melittin. Following mechanistic studies revealed that Lytx-Pa2a disrupts both cytoplasmic and outer membranes of bacteria while simultaneously inducing the accumulation of reactive oxygen species. The peptide exerted no significant toxicity when treated to human primary cells, murine macrophages, and bovine red blood cells. Moreover, Lytx-Pa2a alleviated lipopolysaccharide-induced inflammation in mouse macrophages by suppressing the expression of inflammatory mediators. These findings not only suggested that Lytx-Pa2a with dual activity can be utilized as a new antimicrobial agent for infectious diseases but also demonstrated the implementation of in silico methods for discovering a novel functional peptide, which may enhance the future utilization of biological resources. Full article
(This article belongs to the Special Issue Antimicrobial Peptides from Natural Sources to Synthetic Optimization)
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15 pages, 3597 KiB  
Article
D- and N-Methyl Amino Acids for Modulating the Therapeutic Properties of Antimicrobial Peptides and Lipopeptides
by Maria Veronica Humpola, Roque Spinelli, Melina Erben, Virginia Perdomo, Georgina Guadalupe Tonarelli, Fernando Albericio and Alvaro Sebastian Siano
Antibiotics 2023, 12(5), 821; https://doi.org/10.3390/antibiotics12050821 - 27 Apr 2023
Viewed by 1206
Abstract
Here we designed and synthesized analogs of two antimicrobial peptides, namely C10:0-A2, a lipopeptide, and TA4, a cationic α-helical amphipathic peptide, and used non-proteinogenic amino acids to improve their therapeutic properties. The physicochemical properties of these analogs were analyzed, including their retention time, [...] Read more.
Here we designed and synthesized analogs of two antimicrobial peptides, namely C10:0-A2, a lipopeptide, and TA4, a cationic α-helical amphipathic peptide, and used non-proteinogenic amino acids to improve their therapeutic properties. The physicochemical properties of these analogs were analyzed, including their retention time, hydrophobicity, and critical micelle concentration, as well as their antimicrobial activity against gram-positive and gram-negative bacteria and yeast. Our results showed that substitution with D- and N-methyl amino acids could be a useful strategy to modulate the therapeutic properties of antimicrobial peptides and lipopeptides, including enhancing stability against enzymatic degradation. The study provides insights into the design and optimization of antimicrobial peptides to achieve improved stability and therapeutic efficacy. TA4(dK), C10:0-A2(6-NMeLys), and C10:0-A2(9-NMeLys) were identified as the most promising molecules for further studies. Full article
(This article belongs to the Special Issue Antimicrobial Peptides from Natural Sources to Synthetic Optimization)
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13 pages, 2312 KiB  
Article
The Antimicrobial Peptide Octopromycin Suppresses Biofilm Formation and Quorum Sensing in Acinetobacter baumannii
by Dinusha Chathurangi Rajapaksha, Shan Lakmal Edirisinghe, Chamilani Nikapitiya, Ilson Whang and Mahanama De Zoysa
Antibiotics 2023, 12(3), 623; https://doi.org/10.3390/antibiotics12030623 - 21 Mar 2023
Cited by 6 | Viewed by 2063
Abstract
Acinetobacter baumannii is an opportunistic bacterial pathogen that causes severe infections in immunocompromised individuals. A. baumannii forms biofilm and produces extracellular matrix, which supports bacteria to survive under harsh conditions and be resistant to antibacterial treatments. In the present study, we investigated the [...] Read more.
Acinetobacter baumannii is an opportunistic bacterial pathogen that causes severe infections in immunocompromised individuals. A. baumannii forms biofilm and produces extracellular matrix, which supports bacteria to survive under harsh conditions and be resistant to antibacterial treatments. In the present study, we investigated the biofilm and quorum-sensing inhibitory effects of antimicrobial peptide, octopromycin in A. baumannii. Field emission-scanning electron microscopy results clearly showed significantly reduced biofilm mass and caused a collapse in biofilm architecture at the minimum inhibitory concentration (50 µg/mL) and minimum bactericidal concentration (200 µg/mL) of octopromycin. Antibiotic-resistant persister cells of A. baumannii were successfully killed by octopromycin treatment, and it inhibited violacein production in Chromobacterium violaceum in a concentration-dependent manner. Octopromycin also inhibited alginate production, surface movements (swarming and swimming), and twitching motility of A. baumannnii, confirming its anti-quorum-sensing activity. Multiple metabolic pathways, two-component regulation systems, quorum-sensing, and antibiotic synthesis-related pathways in A. baumannii biofilms were strongly affected by octopromycin treatment. The collective findings indicate that the antibacterial peptide octopromycin may control A. baumannii biofilms through multi-target interactions. Octopromycin could be a desirable therapeutic option for the prevention and control of A. baumannii infections. Full article
(This article belongs to the Special Issue Antimicrobial Peptides from Natural Sources to Synthetic Optimization)
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18 pages, 2648 KiB  
Article
Comparative Evaluation of Existing and Rationally Designed Novel Antimicrobial Peptides for Treatment of Skin and Soft Tissue Infections
by Anna Ramata-Stunda, Martins Boroduskis, Elza Kaktina, Liene Patetko, Uldis Kalnenieks, Zane Lasa, Marta Rubina, Inese Strazdina, Gints Kalnins and Reinis Rutkis
Antibiotics 2023, 12(3), 551; https://doi.org/10.3390/antibiotics12030551 - 10 Mar 2023
Viewed by 1992
Abstract
Skin and soft tissue infections (SSTIs) and acne are among the most common skin conditions in primary care. SSTIs caused by ESKAPE pathogens (Enterococcus faecium, Staphylococcus aureus, Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa, and Enterobacter sp.) can [...] Read more.
Skin and soft tissue infections (SSTIs) and acne are among the most common skin conditions in primary care. SSTIs caused by ESKAPE pathogens (Enterococcus faecium, Staphylococcus aureus, Klebsiella pneumoniae, Acinetobacter baumannii, Pseudomonas aeruginosa, and Enterobacter sp.) can range in severity, and treating them is becoming increasingly challenging due to the growing number of antibiotic-resistant pathogens. There is also a rise in antibiotic-resistant strains of Cutibacterium acne, which plays a role in the development of acne. Antimicrobial peptides (AMPs) are considered to be a promising solution to the challenges posed by antibiotic resistance. In this study, six new AMPs were rationally designed and compared to five existing peptides. The MIC values against E. coli, P. aeruginosa, K. pneumoniae, E. faecium, S. aureus, and C. acnes were determined, and the peptides were evaluated for cytotoxicity using Balb/c 3T3 cells and dermal fibroblasts, as well as for hemolytic activity. The interaction with bacterial membranes and the effect on TNF-α and IL-10 secretion were also evaluated for selected peptides. Of the tested peptides, RP556 showed high broad-spectrum antibacterial activity without inducing cytotoxicity or hemolysis, and it stimulated the production of IL-10 in LPS-stimulated peripheral blood mononuclear cells. Four of the novel AMPs showed pronounced specificity against C. acnes, with MIC values (0.3–0.5 μg/mL) below the concentrations that were cytotoxic or hemolytic. Full article
(This article belongs to the Special Issue Antimicrobial Peptides from Natural Sources to Synthetic Optimization)
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14 pages, 1748 KiB  
Article
In Vitro Antifungal Activity of Chimeric Peptides Derived from Bovine Lactoferricin and Buforin II against Cryptococcus neoformans var. grubii
by Silvia Katherine Carvajal, Yerly Vargas-Casanova, Héctor Manuel Pineda-Castañeda, Javier Eduardo García-Castañeda, Zuly Jenny Rivera-Monroy and Claudia Marcela Parra-Giraldo
Antibiotics 2022, 11(12), 1819; https://doi.org/10.3390/antibiotics11121819 - 15 Dec 2022
Viewed by 1286
Abstract
Cryptococcosis is associated with high rates of morbidity and mortality. The limited number of antifungal agents, their toxicity, and the difficulty of these molecules in crossing the blood–brain barrier have made the exploration of new therapeutic candidates against Cryptococcus neoformans a priority task. [...] Read more.
Cryptococcosis is associated with high rates of morbidity and mortality. The limited number of antifungal agents, their toxicity, and the difficulty of these molecules in crossing the blood–brain barrier have made the exploration of new therapeutic candidates against Cryptococcus neoformans a priority task. To optimize the antimicrobial functionality and improve the physicochemical properties of AMPs, chemical strategies include combinations of peptide fragments into one. This study aimed to evaluate the binding of the minimum activity motif of bovine lactoferricin (LfcinB) and buforin II (BFII) against C. neoformans var. grubii. The antifungal activity against these chimeras was evaluated against (i) the reference strain H99, (ii) three Colombian clinical strains, and (iii) eleven mutant strains, with the aim of evaluating the possible antifungal target. We found high activity against these strains, with a MIC between 6.25 and 12.5 µg/mL. Studies were carried out to evaluate the effect of the combination of fluconazole treatments, finding a synergistic effect. Finally, when fibroblast cells were treated with 12.5 µg/mL of the chimeras, a viability of more than 65% was found. The results obtained in this study identify these chimeras as potential antifungal molecules for future therapeutic applications against cryptococcosis. Full article
(This article belongs to the Special Issue Antimicrobial Peptides from Natural Sources to Synthetic Optimization)
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13 pages, 984 KiB  
Article
Chimeric Peptides Derived from Bovine Lactoferricin and Buforin II: Antifungal Activity against Reference Strains and Clinical Isolates of Candida spp.
by Katherine Aguirre-Guataqui, Mateo Márquez-Torres, Héctor Manuel Pineda-Castañeda, Yerly Vargas-Casanova, Andrés Ceballos-Garzon, Zuly Jenny Rivera-Monroy, Javier Eduardo García-Castañeda and Claudia Marcela Parra-Giraldo
Antibiotics 2022, 11(11), 1561; https://doi.org/10.3390/antibiotics11111561 - 05 Nov 2022
Cited by 3 | Viewed by 1809
Abstract
Antimicrobial peptides (AMPs) are considered to be a valuable source for the identification and/or design of promising candidates for the development of antifungal treatments, since they have advantages such as lower tendency to induce resistance, ease of production, and high purity and safety. [...] Read more.
Antimicrobial peptides (AMPs) are considered to be a valuable source for the identification and/or design of promising candidates for the development of antifungal treatments, since they have advantages such as lower tendency to induce resistance, ease of production, and high purity and safety. Bovine lactoferricin (LfcinB) and Buforin II (BFII) are AMPs to which great antimicrobial potential has been attributed. The minimum motives with antimicrobial activity derived from LfcinB and BFII are RRWQWR and RLLR, respectively. Nine chimeras containing the minimum motives of both peptides were synthesized and their antifungal activity against fluconazole (FLC)-sensitive and resistant C. albicans, C. glabrata, and C. auris strains was evaluated. The results showed that peptides C9: (RRWQWR)2K-Ahx-RLLRRRLLR and C6: KKWQWK-Ahx-RLLRRLLR exhibited the greatest antifungal activity against two strains of C. albicans, a FLC-sensitive reference strain and a FLC-resistant clinical isolate; no medically significant results were observed with the other chimeras evaluated (MIC ~200 μg/mL). The chimera C6 was also active against sensitive and resistant strains of C. glabrata and C. auris. The combination of branched polyvalent chimeras together with FLC showed a synergistic effect against C. albicans. In addition to exhibiting antifungal activity against reference strains and clinical isolates of Candida spp., they also showed antibacterial activity against both Gram-positive and Gram-negative bacteria, suggesting that these chimeras exhibit a broad antimicrobial spectrum and can be considered to be promising molecules for therapeutic applications. Full article
(This article belongs to the Special Issue Antimicrobial Peptides from Natural Sources to Synthetic Optimization)
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9 pages, 2128 KiB  
Article
Antifungal Activity of Avocado Seed Recombinant GASA/Snakin PaSn
by Marco Antonio Hernández-Martínez, Luis María Suárez-Rodríguez, Joel Edmundo López-Meza, Alejandra Ochoa-Zarzosa, Rafael Salgado-Garciglia, Silvia Patricia Fernández-Pavia and Rodolfo López-Gómez
Antibiotics 2022, 11(11), 1558; https://doi.org/10.3390/antibiotics11111558 - 05 Nov 2022
Cited by 2 | Viewed by 1637
Abstract
The avocado fruit (Persea americana) has become a significant fruit in the human diet for its nutritional properties. However, the seed is a source of bioactive molecules and has been poorly utilized. Previously, we reported that the PaSn gene is expressed [...] Read more.
The avocado fruit (Persea americana) has become a significant fruit in the human diet for its nutritional properties. However, the seed is a source of bioactive molecules and has been poorly utilized. Previously, we reported that the PaSn gene is expressed in the avocado seeds, a cysteine-rich antimicrobial peptide (GASA/Snakin), and demonstrated its antibacterial activity. In this work, we report the recombinant production of PaSn in the Escherichia coli system and evaluate its antifungal activity against plant and human pathogen fungi. The recombinant peptide showed antifungal activity at 200 μg/mL against phytopathogens Colletotrichum gloeosporioides and Fusarium oxysporum and human pathogens Candida albicans and C. glabrata. Our results demonstrate the usefulness of a prokaryotic expression system for avocado antimicrobial peptide production. In conclusion, the snakin PaSn could be helpful in the control of postharvest avocado and other fruits’ fungal diseases and human fungal pathogens. Full article
(This article belongs to the Special Issue Antimicrobial Peptides from Natural Sources to Synthetic Optimization)
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