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Applied Sciences
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Antimicrobial Peptides: Discovery, Design and Novel Therapeutic Strategies 2019
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Antimicrobial Peptides: Discovery, Design and Novel Therapeutic Strategies 2019

A special issue of Applied Sciences (ISSN 2076-3417). This special issue belongs to the section "Applied Biosciences and Bioengineering".

Deadline for manuscript submissions: closed (31 March 2020) | Viewed by 10274

Special Issue Editors

Dr. Lidia Feliu

E-Mail Website
Guest Editor
Department of Chemistry, University of Girona, Campus Montilivi, 17004 Girona, Spain
Interests: peptides; heterocyclic compounds; synthesis and structure of natural products; design, synthesis, and study of new drugs; chemical control of plant diseases
Assoc. Prof. Dr. Marta Planas

E-Mail Website
Guest Editor
Department of Chemistry, University of Girona, Campus Montilivi, Girona, Spain
Interests: peptides; heterocyclic compounds; synthesis and structure of natural products; design, synthesis, and study of new drugs; chemical control of plant diseases

Special Issue Information

Dear Colleagues,

In the past several decades, antimicrobial peptides have emerged as valuable therapeutic agents with a wide range of applications. They have been isolated from natural sources or obtained using chemical methodologies. Synthetic antimicrobial peptides can be designed through the modification of natural sequences or by using de novo design strategies. The latter approach is usually based on the structural features of antimicrobial peptides described to be crucial for their mechanism of action. The efforts devoted to this research have resulted in peptides with interesting properties that have led to advances in fields with high social impact, namely agriculture, medicine, veterinary medicine, and the food industry.

The aim of this Special Issue is to gather original research articles focused on all aspects of antimicrobial peptide chemistry and biology: isolation and characterization, design of new analogues, synthetic methodologies, mechanistic studies, and biological applications. This Issue will contribute to update the knowledge of this research field, and will be of interest for scientists from several disciplines.

Assoc. Prof. Dr. Lidia Feliu
Assoc. Prof. Dr. Marta Planas
Guest Editors

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Keywords

  • isolation and characterization of antimicrobial peptides
  • design of antimicrobial peptides, including computational methods
  • synthetic methodology
  • combinatorial peptide research: libraries of antimicrobial peptides
  • mechanism of action of antimicrobial peptides
  • antimicrobial peptides in plant diseases
  • antimicrobial peptides with clinical or veterinary application
  • antimicrobial peptides in food chemistry
  • new perspectives of antimicrobial peptides

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Published Papers (3 papers)

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Research

14 pages, 2100 KiB  
Article
Antioxidant and Antimicrobial Activity of Porcine Liver Hydrolysates Using Flavourzyme
by Paula Borrajo, María López-Pedrouso, Daniel Franco, Mirian Pateiro and José M. Lorenzo
Appl. Sci. 2020, 10(11), 3950; https://doi.org/10.3390/app10113950 - 6 Jun 2020
Cited by 15 | Viewed by 3694
Abstract
Oxidative stress is implicated in human diseases including cancer or neurodegenerative diseases. On the other hand, lipid and microbial spoilage are the main issues of food degradation. Bioactive peptides with antioxidant and antimicrobial activity could solve both problems and create an opportunity to [...] Read more.
Oxidative stress is implicated in human diseases including cancer or neurodegenerative diseases. On the other hand, lipid and microbial spoilage are the main issues of food degradation. Bioactive peptides with antioxidant and antimicrobial activity could solve both problems and create an opportunity to improve the sustainability of the meat industry. Recently, meat by-products are subject of numerous studies to produce antioxidant peptides, highlighting pork liver as a potential source of hydrolysates. To achieve this purpose, pork liver was digested with Flavourzyme at four reaction times (4, 6, 8, and 10 h) and filtered with cut-offs of 5, 10, and 30-kDa molecular weight. Monitoring hydrolysis with SDS-PAGE showed that the reaction was almost complete. Free amino acid profile exhibited that aliphatic and aromatic amino acids were released in a higher amount at longer reaction times. Heat map analysis demonstrated that a hydrolysis time beyond 6 h, displayed a differential amino acid pattern enabling us to optimize the enzymatic reaction. Antioxidant activity was assessed using ABTS, DPPH, FRAP, and ORAC tests, while antimicrobial assay was carried out against Gram-positive and Gram-negative. ABTS and DPPH values revealed that hydrolysates showed a high antioxidant capacity, as well as an inhibition of growth of Brochothrix thermosphata particularly 30 kDa hydrolysates. Full article
(This article belongs to the Special Issue Antimicrobial Peptides: Discovery, Design and Novel Therapeutic Strategies 2019)
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11 pages, 3733 KiB  
Article
Enhanced Antifungal Activity of Engineered Proteins via Swapping between Thioredoxin H2 and H3
by Jin-Young Kim, Yong Hun Chi, Il Ryong Kim, Heabin Kim, Ji Hyun Jung, Seong-Cheol Park, Mi-Kyeong Jang, Sang Yeol Lee and Jung Ro Lee
Appl. Sci. 2019, 9(22), 4766; https://doi.org/10.3390/app9224766 - 8 Nov 2019
Cited by 1 | Viewed by 2739
Abstract
Thioredoxins (Trxs) are proteins that act as antioxidants by facilitating the reduction of other proteins and are highly conserved in all organisms. Plant H-type Trx isoforms have different structures and perform multiple functions. Previous studies have reported that the low molecular weight AtTrx-H2 [...] Read more.
Thioredoxins (Trxs) are proteins that act as antioxidants by facilitating the reduction of other proteins and are highly conserved in all organisms. Plant H-type Trx isoforms have different structures and perform multiple functions. Previous studies have reported that the low molecular weight AtTrx-H2 acts as a disulfide reductase and the high molecular weight AtTrx-H3 functions as an oxidoreductase and a molecular chaperone. In this study, we compared the antifungal activities of Arabidopsis Trx-H2 and -H3 with engineered proteins 2N3C and 3N2C via domain-swapping between the N- and C-terminal regions of Trx-H2 and -H3. All AtTrx-H variant proteins inhibited cell growth of various pathogenic fungal strains at pH 5.2 and pH 7.2 and showed significant intracellular accumulation in the fungal cells. Interestingly, only two engineered proteins penetrated the fungal cell wall and membrane, indicating their ability to destabilize the fungal cell membrane before internalization into the cytosol. To our knowledge, this is the first study that demonstrates novel functions of plant antioxidants AtTrx-H2 and -H3 as antifungal proteins and shows their enhanced activity using the domain swapping technique. Full article
(This article belongs to the Special Issue Antimicrobial Peptides: Discovery, Design and Novel Therapeutic Strategies 2019)
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15 pages, 6186 KiB  
Article
A Comparative Study on Interactions of Antimicrobial Peptides L- and D-phenylseptin with 1,2-dimyristoyl-sn-glycero-3-phosphocholine
by Batsaikhan Mijiddorj, Yuta Matsuo, Hisako Sato, Kazuyoshi Ueda and Izuru Kawamura
Appl. Sci. 2019, 9(13), 2601; https://doi.org/10.3390/app9132601 - 27 Jun 2019
Cited by 7 | Viewed by 3211
Abstract
L-phenylseptin (L-Phes) and D-phenylseptin (D-Phes) are amphibian antimicrobial peptides isolated from the skin secretion of Hypsiboas punctatus. In the N-termini, L-Phes and D-Phes contain three consecutive phenylalanine residues, l-Phe-l-Phe-l-Phe and l-Phe-d-Phe-l-Phe, respectively. They [...] Read more.
L-phenylseptin (L-Phes) and D-phenylseptin (D-Phes) are amphibian antimicrobial peptides isolated from the skin secretion of Hypsiboas punctatus. In the N-termini, L-Phes and D-Phes contain three consecutive phenylalanine residues, l-Phe-l-Phe-l-Phe and l-Phe-d-Phe-l-Phe, respectively. They are known to exhibit antimicrobial activity against Staphylococcus aureus, Escherichia coli, Pseudomonas aeruginosa, and Xanthomonas axonopodis pv. Glycines. However, their mechanism of action and the role of the D-amino acid residue have not been elucidated yet. In this study, the interactions of both peptides with 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) were investigated by means of quartz crystal microbalance, circular dichroism, vibrational circular dichroism, 31P solid-state NMR, and molecular dynamics simulation. Both peptides have similar binding constants to the DMPC lipid bilayers, in the order of 106 M−1, and form an α-helix structure in the DMPC lipid bilayers. Both the peptides induce similar changes in the dynamics of DMPC lipids. Thus, in spite of the difference in the conformations caused by the chirality at the N-terminus, the peptides showed similar behavior in the membrane-bound state, experimentally and computationally. Full article
(This article belongs to the Special Issue Antimicrobial Peptides: Discovery, Design and Novel Therapeutic Strategies 2019)
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