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Biomolecules
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State of the Art and Perspectives in Antimicrobial Peptides
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State of the Art and Perspectives in Antimicrobial Peptides

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Molecular Medicine".

Deadline for manuscript submissions: 31 May 2025 | Viewed by 9084

Special Issue Editor

Dr. Annarita Falanga

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Guest Editor
Department of Agricultural Sciences, University of Naples Federico II, 80055 Portici, Italy
Interests: antimicrobial peptide; self-assembling nanostructures based peptides; drug delivery
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Bacterial infections caused by ‘superbugs’ are increasing globally, and conventional antibiotics are becoming less effective against these bacteria. A strong modification of lifestyle is required since we risk reverting back to a pre-antibiotic era in terms of immunological protection. Within this context, antimicrobial peptides (AMPs), a class of small peptides that widely exist in nature and contribute to an organism’s defenses, have attracted researchers’ attention. Perspectives and applications are numerous and cover different fields. Although peptides present some weaknesses in membrane impermeability and poor stability in vivo, due to the intrinsic limitations of amino acids, extensive research has been carried out in terms of the discovery and optimization of peptide drugs in order to overcome these drawbacks. The use of chemical modification and integration of traditional lead peptide discovery methods with novel technologies, such as rational design models, provides a reliable approach for the development of effective and selective lead peptides in a short period of time. Moreover, the design of peptide-based nano-systems opens the door to new and important scenarios.

Prof. Dr. Annarita Falanga
Guest Editor

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Keywords

  • antimicrobial peptides
  • AMPs
  • chemical modification of AMPs
  • function
  • structure
  • synthesis

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Published Papers (6 papers)

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Research

16 pages, 2387 KiB  
Article
In Vitro and In Vivo Evaluation of the De Novo Designed Antimicrobial Peptide P6.2 Against a KPC-Producing P. aeruginosa Clinical Isolate
by Melina M. B. Martinez, Merlina Corleto, Melanie Weschenfeller, Santiago Urrea Montes, Camila N. Salomón, Natalia Gonzalez, Matías Garavaglia, Diego Faccone and Paulo C. Maffía
Biomolecules 2025, 15(3), 339; https://doi.org/10.3390/biom15030339 - 27 Feb 2025
Viewed by 628
Abstract
The antimicrobial peptide P6.2 was previously de novo designed as an alpha helix cationic amphipathic molecule. In previous work, we have shown that this peptide displayed significant antimicrobial activity against both Gram-positive (Staphylococcus aureus) and Gram-negative (Pseudomonas aeruginosa) bacteria. [...] Read more.
The antimicrobial peptide P6.2 was previously de novo designed as an alpha helix cationic amphipathic molecule. In previous work, we have shown that this peptide displayed significant antimicrobial activity against both Gram-positive (Staphylococcus aureus) and Gram-negative (Pseudomonas aeruginosa) bacteria. However, while P6.2 lacked biofilm-inhibiting properties against the P. aeruginosa strain PA01, it displayed anti-inflammatory effects in a murine acute lung infection model challenged with this pathogen. In this work, the peptide P6.2 antimicrobial activity and its possible synergy with meropenem were evaluated both in vitro and in vivo using a Galleria mellonella infection model against a carbapenem-resistant KPC-producing clinical isolate of P. aeruginosa. Firstly, the cytotoxic effect of the peptide on A549 and RAW264.7 cell lines was assayed, showing no cytotoxicity at 64 µg/mL and below. Then, the MIC (minimal inhibitory concentration) and bactericidal effect against the carbapenemase-producing strain P. aeruginosa M13513 strain were determined. P6.2 showed a MIC between 32 and 64 µg/mL, and a rapid bactericidal activity against this strain (less than 45 min). The peptide stability at different temperatures and in bovine serum at 37 °C was also analyzed, showing good stability and almost no degradation after 15 min of incubation at 100 °C or 24 h at 37 °C in serum, respectively. The antibiofilm activity was also evaluated, and although the peptide did not show biofilm inhibitory activity, it did demonstrate biofilm disruptive activity, together with bactericidal activity inside the pre-formed biofilm. The possible synergistic effect with the carbapenem meropenem was then analyzed in vitro by killing kinetics, revealing a synergistic interaction between P6.2 and the antibiotic against this strain. Finally, P6.2 was evaluated in vivo in the Galleria mellonella larvae infection model. Interestingly, in G. mellonella, P6.2 alone did not completely clear the infection caused by P. aeruginosa M13513. However, when combined with meropenem, P6.2 demonstrated a synergistic effect, leading to increased survival rates in infected larvae. The results presented here highlight the potential that this peptide displays when used in combination with carbapenems against a clinically relevant KPC-producing P. aeruginosa. Full article
(This article belongs to the Special Issue State of the Art and Perspectives in Antimicrobial Peptides)
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16 pages, 4673 KiB  
Communication
Antimicrobial Activity of the Peptide C14R Against Ab Initio Growing and Preformed Biofilms of Candida albicans, Candida parapsilosis and Candidozyma auris
by Jan-Christoph Walter, Ann-Kathrin Kissmann, Daniel Gruber, Daniel Alpízar-Pedraza, Ernesto M. Martell-Huguet, Nico Preising, Armando Rodriguez-Alfonso, Ludger Ständker, Christoph Kleber, Wolfgang Knoll, Steffen Stenger, Carolina Firacative and Frank Rosenau
Biomolecules 2025, 15(3), 322; https://doi.org/10.3390/biom15030322 - 21 Feb 2025
Viewed by 840
Abstract
Biofilms are the predominant lifeforms of microorganisms, contributing to over 80% of infections, including those caused by Candida species like C. albicans, C. parapsilosis and Candidozyma auris. These species form biofilms on medical devices, making infections challenging to treat, especially with [...] Read more.
Biofilms are the predominant lifeforms of microorganisms, contributing to over 80% of infections, including those caused by Candida species like C. albicans, C. parapsilosis and Candidozyma auris. These species form biofilms on medical devices, making infections challenging to treat, especially with the rise in drug-resistant strains. Candida infections, particularly hospital-acquired ones, are a significant health threat due to their resistance to antifungals and the risk of developing systemic infections (i.e., sepsis). We have previously shown that C14R reduces the viability of C. albicans and C. auris, but not of C. parapsilosis. Here, we show that C14R not only inhibits viability by pore formation, shown in a resazurin reduction assay, and in a C. parapsilosis and fluorescence-based permeabilization assay, but it also halts biofilm maturation and significantly reduces the biomass of preformed biofilms by over 70%. These findings suggest C14R could be an effective option for treating severe fungal infections, offering a potential new treatment approach for biofilm-related diseases. Further research is needed to fully understand its biofilm dispersal potential and to optimize its use for future applications as an antifungal in clinical settings. Full article
(This article belongs to the Special Issue State of the Art and Perspectives in Antimicrobial Peptides)
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20 pages, 11323 KiB  
Article
Senegalin-2: A Novel Hexadecapeptide from Kassina senegalensis with Antibacterial and Muscle Relaxant Activities, and Its Derivative Senegalin-2BK as a Bradykinin Antagonist
by Yueyang Lu, Yanguo Zhu, Chengbang Ma, Lei Wang, Mei Zhou, Tianbao Chen, Xiaonan Ma, Xu Zhang and Zhimin Fan
Biomolecules 2025, 15(1), 30; https://doi.org/10.3390/biom15010030 - 30 Dec 2024
Cited by 4 | Viewed by 872
Abstract
The amphibian skin secretions are excellent sources of bioactive peptides, some of which and their derivatives exhibit multiple properties, including antibacterial and antagonism against bradykinin. A novel peptide Senegalin-2 was isolated from the skin secretions of Kassina senegalensis frog. Senegalin-2 relaxed rat bladder [...] Read more.
The amphibian skin secretions are excellent sources of bioactive peptides, some of which and their derivatives exhibit multiple properties, including antibacterial and antagonism against bradykinin. A novel peptide Senegalin-2 was isolated from the skin secretions of Kassina senegalensis frog. Senegalin-2 relaxed rat bladder smooth muscle (EC50 17.94 nM) and ileum smooth muscle (EC50 135 nM), inhibited S. aureus and MRSA at 2 μM, and exhibited low hemolytic activity with no cytotoxicity. To design effective bradykinin antagonists, Senegalin-2 was conjugated with bradykinin to synthesize Senegalin-2BK. This modification retained potent activity against Gram-positive bacteria. Compared to Senegalin-2, Senegalin-2BK significantly reduced hemolysis and exhibited a more than threefold increase in the selectivity index. Furthermore, Senegalin-2BK contracted the bladder (EC50 2.83 μM) and ileum (EC50 56.64 nM)’s smooth muscle. The pretreatment with 10−7 M Senegalin-2BK reduced the 10−6 M bradykinin contraction on the bladder by over 70%. In conclusion, Senegalin-2 has dual functionalities as an antibacterial agent and muscle relaxant, positioning it as a potential therapeutic candidate for managing overactive bladder. As a synthetically derived bradykinin antagonist and myotropic peptide with antibacterial properties, Senegalin-2BK shows promise in effective therapies for relieving pain, inflammation, and addressing muscular disorders such as urinary retention, constipation, and infections. Full article
(This article belongs to the Special Issue State of the Art and Perspectives in Antimicrobial Peptides)
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22 pages, 7650 KiB  
Article
Identification of Multifunctional Putative Bioactive Peptides in the Insect Model Red Palm Weevil (Rhynchophorus ferrugineus)
by Carmen Scieuzo, Roberta Rinaldi, Fabiana Giglio, Rosanna Salvia, Mohammed Ali AlSaleh, Jernej Jakše, Arnab Pain, Binu Antony and Patrizia Falabella
Biomolecules 2024, 14(10), 1332; https://doi.org/10.3390/biom14101332 - 19 Oct 2024
Cited by 2 | Viewed by 2141
Abstract
Innate immunity, the body’s initial defense against bacteria, fungi, and viruses, heavily depends on antimicrobial peptides (AMPs), which are small molecules produced by all living organisms. Insects, with their vast biodiversity, are one of the most abundant and innovative sources of AMPs. In [...] Read more.
Innate immunity, the body’s initial defense against bacteria, fungi, and viruses, heavily depends on antimicrobial peptides (AMPs), which are small molecules produced by all living organisms. Insects, with their vast biodiversity, are one of the most abundant and innovative sources of AMPs. In this study, AMPs from the red palm weevil (RPW) Rhynchophorus ferrugineus (Coleoptera: Curculionidae), a known invasive pest of palm species, were examined. The AMPs were identified in the transcriptomes from different body parts of male and female adults, under different experimental conditions, including specimens collected from the field and those reared in the laboratory. The RPW transcriptomes were examined to predict antimicrobial activity, and all sequences putatively encoding AMPs were analyzed using several machine learning algorithms available in the CAMPR3 database. Additionally, anticancer, antiviral, and antifungal activity of the peptides were predicted using iACP, AVPpred, and Antifp server tools, respectively. Physicochemical parameters were assessed using the Antimicrobial Peptide Database Calculator and Predictor. From these analyses, 198 putatively active peptides were identified, which can be tested in future studies to validate the in silico predictions. Genome-wide analysis revealed that several AMPs have predominantly emerged through gene duplication. Noticeably, we detect a newly originated defensin allele from an ancestral defensin via the deletion of two amino acids following gene duplication in RPW, which may confer an enhanced resilience to microbial infection. Our study shed light on AMP gene families and shows that high duplication and deletion rates are essential to achieve a diversity of antimicrobial mechanisms; hence, we propose the RPW AMPs as a model for exploring gene duplication and functional variations against microbial infection. Full article
(This article belongs to the Special Issue State of the Art and Perspectives in Antimicrobial Peptides)
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15 pages, 2189 KiB  
Article
Membrane Activity of Melittin and Magainin-I at Low Peptide-to-Lipid Ratio: Different Types of Pores and Translocation Mechanisms
by Marta V. Volovik and Oleg V. Batishchev
Biomolecules 2024, 14(9), 1118; https://doi.org/10.3390/biom14091118 - 4 Sep 2024
Viewed by 1450
Abstract
Antimicrobial peptides (AMPs) are believed to be a prominent alternative to the common antibiotics. However, despite decades of research, there are still no good clinical examples of peptide-based antimicrobial drugs for system application. The main reasons are loss of activity in the human [...] Read more.
Antimicrobial peptides (AMPs) are believed to be a prominent alternative to the common antibiotics. However, despite decades of research, there are still no good clinical examples of peptide-based antimicrobial drugs for system application. The main reasons are loss of activity in the human body, cytotoxicity, and low selectivity. To overcome these challenges, a well-established structure–function relationship for AMPs is critical. In the present study, we focused on the well-known examples of melittin and magainin to investigate in detail the initial stages of AMP interaction with lipid membranes at low peptide-to-lipid ratio. By combining the patch-clamp technique with the bioelectrochemical method of intramembrane field compensation, we showed that these peptides interact with the membrane in different ways: melittin inserts deeper into the lipid bilayer than magainin. This difference led to diversity in pore formation. While magainin, after a threshold concentration, formed the well-known toroidal pores, allowing the translocation of the peptide through the membrane, melittin probably induced predominantly pure lipidic pores with a very low rate of peptide translocation. Thus, our results shed light on the early stages of peptide–membrane interactions and suggest new insights into the structure–function relationship of AMPs based on the depth of their membrane insertion. Full article
(This article belongs to the Special Issue State of the Art and Perspectives in Antimicrobial Peptides)
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17 pages, 4186 KiB  
Article
Functional Analyses of Three Targeted DNA Antimicrobial Peptides Derived from Goats
by Aili Wang, Mengying Zhou, Qian Chen, Hui Jin, Gaochi Xu, Ruiyin Guo, Jianmin Wang and Ren Lai
Biomolecules 2023, 13(10), 1453; https://doi.org/10.3390/biom13101453 - 27 Sep 2023
Cited by 2 | Viewed by 1984
Abstract
With the increase in drug-resistant bacteria, new antibacterial drugs have emerged as a prominent area of research and development. Antimicrobial peptides (AMPs), as innate immune agents, have garnered significant attention due to their potent, rapid, and broad-spectrum antibacterial activity. This study focused on [...] Read more.
With the increase in drug-resistant bacteria, new antibacterial drugs have emerged as a prominent area of research and development. Antimicrobial peptides (AMPs), as innate immune agents, have garnered significant attention due to their potent, rapid, and broad-spectrum antibacterial activity. This study focused on investigating the functionality of three AMPs (CATH 1, CATH 2, and MAP34-B) derived from goat submandibular glands. Among these AMPs, CATH 2 and MAP34-B exhibited direct antibacterial activity against both Gram-negative and Gram-positive bacteria, primarily targeting the bacterial membrane. Additionally, these two AMPs were found to have the potential to induce reactive oxygen species (ROS) production in bacterial cells and interact with bacterial genome DNA, which may play a crucial role in their mechanisms of action. Furthermore, both CATH 1 and CATH 2 demonstrated significant antioxidant activity, and all three AMPs exhibited potential anti-inflammatory activity. Importantly, the cytotoxic activity of these AMPs against mammalian cells was found to be weak, and their hemolytic activity was extremely low. Overall, the characteristics of these three AMPs found in goat submandibular glands offer new insights for the study of host protection from an immunological perspective. They hold promise as potential candidates for the development of novel antibacterial agents, particularly in the context of combating drug-resistant bacteria. Full article
(This article belongs to the Special Issue State of the Art and Perspectives in Antimicrobial Peptides)
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