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Antibiotics
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The Century-Long Journey of Peptide-Based Drugs
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The Century-Long Journey of Peptide-Based Drugs

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

Deadline for manuscript submissions: closed (30 September 2023) | Viewed by 24184

Special Issue Editor

Dr. José Rafael De Almeida

E-Mail Website
Guest Editor
Biomolecules Discovery Group, Universidad Regional Amazónica Ikiam, Km 8 Via Muyuna, Tena 150101, Ecuador
Interests: peptides; venomics; snake venom; toxins; anti-infective agents
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Peptides are low-molecular-weight bioactive molecules with multidimensional biological properties. The first injection of insulin in 1922 marked the beginning of the era of therapeutic peptides. Developing peptide-based drugs is challenging and characterized by several obstacles, such as low oral bioavailability and a short half-life. In contrast, the current landscape of peptides in the pharmaceutical industry has shown many applications of these molecules, leading to increased FDA drug approval and generating billions in revenue. The development of technologies for the rational design and screening of the biological and toxic potential of these small molecules has garnered significant interest among biotechnology-based and medical companies. This Special Issue seeks to bring together a collection of therapeutic and biotechnological applications of natural and synthetic peptides to showcase the latest advances in this field. We invite you to submit an original article, short communication, or review article to this Special Issue, focusing on the whole spectrum of therapeutic peptides.

Dr. José Rafael De Almeida
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.

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Published Papers (6 papers)

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Editorial

Jump to: Research, Review

5 pages, 499 KiB  
Editorial
The Century-Long Journey of Peptide-Based Drugs
by José R. Almeida
Antibiotics 2024, 13(3), 196; https://doi.org/10.3390/antibiotics13030196 - 20 Feb 2024
Cited by 1 | Viewed by 2549
Abstract
The pioneering medical application of peptides as therapeutics began approximately a century ago; however, they remain clinically relevant candidates garnering more attention on the drug development agenda [...] Full article
(This article belongs to the Special Issue The Century-Long Journey of Peptide-Based Drugs)
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Research

Jump to: Editorial, Review

19 pages, 5103 KiB  
Article
Antibacterial and Antiviral Properties of Chenopodin-Derived Synthetic Peptides
by Marcia L. Feijoo-Coronel, Bruno Mendes, David Ramírez, Carlos Peña-Varas, Nina Q. E. de los Monteros-Silva, Carolina Proaño-Bolaños, Leonardo Camilo de Oliveira, Diego Fernandes Lívio, José Antônio da Silva, José Maurício S. F. da Silva, Marília Gabriella A. G. Pereira, Marina Q. R. B. Rodrigues, Mauro M. Teixeira, Paulo Afonso Granjeiro, Ketan Patel, Sakthivel Vaiyapuri and José R. Almeida
Antibiotics 2024, 13(1), 78; https://doi.org/10.3390/antibiotics13010078 - 14 Jan 2024
Cited by 6 | Viewed by 11109
Abstract
Antimicrobial peptides have been developed based on plant-derived molecular scaffolds for the treatment of infectious diseases. Chenopodin is an abundant seed storage protein in quinoa, an Andean plant with high nutritional and therapeutic properties. Here, we used computer- and physicochemical-based strategies and designed [...] Read more.
Antimicrobial peptides have been developed based on plant-derived molecular scaffolds for the treatment of infectious diseases. Chenopodin is an abundant seed storage protein in quinoa, an Andean plant with high nutritional and therapeutic properties. Here, we used computer- and physicochemical-based strategies and designed four peptides derived from the primary structure of Chenopodin. Two peptides reproduce natural fragments of 14 amino acids from Chenopodin, named Chen1 and Chen2, and two engineered peptides of the same length were designed based on the Chen1 sequence. The two amino acids of Chen1 containing amide side chains were replaced by arginine (ChenR) or tryptophan (ChenW) to generate engineered cationic and hydrophobic peptides. The evaluation of these 14-mer peptides on Staphylococcus aureus and Escherichia coli showed that Chen1 does not have antibacterial activity up to 512 µM against these strains, while other peptides exhibited antibacterial effects at lower concentrations. The chemical substitutions of glutamine and asparagine by amino acids with cationic or aromatic side chains significantly favoured their antibacterial effects. These peptides did not show significant hemolytic activity. The fluorescence microscopy analysis highlighted the membranolytic nature of Chenopodin-derived peptides. Using molecular dynamic simulations, we found that a pore is formed when multiple peptides are assembled in the membrane. Whereas, some of them form secondary structures when interacting with the membrane, allowing water translocations during the simulations. Finally, Chen2 and ChenR significantly reduced SARS-CoV-2 infection. These findings demonstrate that Chenopodin is a highly useful template for the design, engineering, and manufacturing of non-toxic, antibacterial, and antiviral peptides. Full article
(This article belongs to the Special Issue The Century-Long Journey of Peptide-Based Drugs)
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15 pages, 2056 KiB  
Article
In Vitro Antifungal Activity of Three Synthetic Peptides against Candida auris and Other Candida Species of Medical Importance
by Richar Torres, Adriana Barreto-Santamaría, Gabriela Arévalo-Pinzón, Carolina Firacative, Beatriz L. Gómez, Patricia Escandón, Manuel Alfonso Patarroyo and Julián E. Muñoz
Antibiotics 2023, 12(8), 1234; https://doi.org/10.3390/antibiotics12081234 - 26 Jul 2023
Cited by 3 | Viewed by 1786
Abstract
Candidiasis is an opportunistic infection affecting immunosuppressed and hospitalized patients, with mortality rates approaching 40% in Colombia. The growing pharmacological resistance of Candida species and the emergence of multidrug-resistant Candida auris are major public health problems. Therefore, different antimicrobial peptides (AMPs) are being investigated [...] Read more.
Candidiasis is an opportunistic infection affecting immunosuppressed and hospitalized patients, with mortality rates approaching 40% in Colombia. The growing pharmacological resistance of Candida species and the emergence of multidrug-resistant Candida auris are major public health problems. Therefore, different antimicrobial peptides (AMPs) are being investigated as therapeutic alternatives to control candidiasis effectively and safely. This work aimed to evaluate the in vitro antifungal activity of three synthetic AMPs, PNR20, PNR20-1, and 35409, against ATCC reference strains of Candida albicans, Candida glabrata, Candida parapsilosis, Candida krusei, and Candida tropicalis, and clinical isolates of C. auris. Antifungal susceptibility testing, determined by broth microdilution, showed that the AMPs have antifungal activity against planktonic cells of all Candida species evaluated. In C. auris and C. albicans, the peptides had an effect on biofilm formation and cell viability, as determined by the XTT assay and flow cytometry, respectively. Also, morphological alterations in the membrane and at the intracellular level of these species were induced by the peptides, as observed by transmission electron microscopy. In vitro, the AMPs had no cytotoxicity against L929 murine fibroblasts. Our results showed that the evaluated AMPs are potential therapeutic alternatives against the most important Candida species in Colombia and the world. Full article
(This article belongs to the Special Issue The Century-Long Journey of Peptide-Based Drugs)
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14 pages, 1917 KiB  
Article
Mechanisms of Antimicrobial Peptides from Bagasse against Human Pathogenic Bacteria
by Thitiporn Ditsawanon, Narumon Phaonakrob and Sittiruk Roytrakul
Antibiotics 2023, 12(3), 448; https://doi.org/10.3390/antibiotics12030448 - 23 Feb 2023
Viewed by 1921
Abstract
Nonedible agricultural wastes (agricultural wastes, agro-industrial wastes, and fishery wastes) were chosen as potential sources of antimicrobial peptides and evaluated for antibacterial efficiency against human pathogens. Specifically, protein hydrolysates were first obtained by hydrolysis with pepsin. Filtrated peptides smaller than 3 kDa were [...] Read more.
Nonedible agricultural wastes (agricultural wastes, agro-industrial wastes, and fishery wastes) were chosen as potential sources of antimicrobial peptides and evaluated for antibacterial efficiency against human pathogens. Specifically, protein hydrolysates were first obtained by hydrolysis with pepsin. Filtrated peptides smaller than 3 kDa were then purified by C18 reversed-phase chromatography, cation exchange chromatography, and off-gel fractionation. NanoLC-MS/MS was used to investigate the amino acid sequences of active peptide candidates. Five candidate peptides were finally chosen for chemical synthesis and evaluation of growth inhibition against human pathogenic bacteria. Two synthetic peptides from bagasse, NLWSNEINQDMAEF (Asn-Leu-Trp-Ser-Asn-Glu-Ile-Asn-Gln-Asp-Met-Ala-Glu-Phe) and VSNCL (Val-Ser-Asn-Cys-Leu), showed the most potent antibacterial activity against three pathogens: Pseudomonas aeruginosa, Bacillus subtilis, and Burkholderia cepacia. The antibacterial mechanisms of these peptides were then examined using shotgun proteomics, which revealed their effects to involve both intracellular-active and membrane-active mechanisms. Further investigation and modification of peptides are needed to increase the efficiency of these peptides against human pathogens. Full article
(This article belongs to the Special Issue The Century-Long Journey of Peptide-Based Drugs)
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Review

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11 pages, 6823 KiB  
Review
Natural and Man-Made Cyclic Peptide-Based Antibiotics
by Shian Lai, Quan Zhang and Lin Jin
Antibiotics 2023, 12(1), 42; https://doi.org/10.3390/antibiotics12010042 - 27 Dec 2022
Cited by 7 | Viewed by 3069
Abstract
In recent years, an increasing number of drug-resistant bacterial strains have been identified due to the abuse of antibiotics, which seriously threatens human and animal health. Antimicrobial peptides (AMPs) have become one of the most effective weapons to solve this problem. AMPs have [...] Read more.
In recent years, an increasing number of drug-resistant bacterial strains have been identified due to the abuse of antibiotics, which seriously threatens human and animal health. Antimicrobial peptides (AMPs) have become one of the most effective weapons to solve this problem. AMPs have little tendency to induce drug resistance and have outstanding antimicrobial effects. The study of AMPs, especially cyclic peptides, has become a hot topic. Among them, macrocyclic AMPs have received extensive attention. This mini-review discusses the structures and functions of the dominant cyclic natural and synthetic AMPs and provides a little outlook on the future direction of cyclic AMPs. Full article
(This article belongs to the Special Issue The Century-Long Journey of Peptide-Based Drugs)
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17 pages, 341 KiB  
Review
Cell-Penetrating Antimicrobial Peptides with Anti-Infective Activity against Intracellular Pathogens
by Gabriela Silva Cruz, Ariane Teixeira dos Santos, Erika Helena Salles de Brito and Gandhi Rádis-Baptista
Antibiotics 2022, 11(12), 1772; https://doi.org/10.3390/antibiotics11121772 - 8 Dec 2022
Cited by 13 | Viewed by 2798
Abstract
Cell-penetrating peptides (CPPs) are natural or engineered peptide sequences with the intrinsic ability to internalize into a diversity of cell types and simultaneously transport hydrophilic molecules and nanomaterials, of which the cellular uptake is often limited. In addition to this primordial activity of [...] Read more.
Cell-penetrating peptides (CPPs) are natural or engineered peptide sequences with the intrinsic ability to internalize into a diversity of cell types and simultaneously transport hydrophilic molecules and nanomaterials, of which the cellular uptake is often limited. In addition to this primordial activity of cell penetration without membrane disruption, multivalent antimicrobial activity accompanies some CPPs. Antimicrobial peptides (AMPs) with cell-penetrability exert their effect intracellularly, and they are of great interest. CPPs with antimicrobial activity (CPAPs) comprise a particular class of bioactive peptides that arise as promising agents against difficult-to-treat intracellular infections. This short review aims to present the antibacterial, antiparasitic, and antiviral effects of various cell-penetrating antimicrobial peptides currently documented. Examples include the antimicrobial effects of different CPAPs against bacteria that can propagate intracellularly, like Staphylococcus sp., Streptococcus sp., Chlamydia trachomatis, Escherichia coli, Mycobacterium sp., Listeria sp., Salmonella sp. among others. CPAPs with antiviral effects that interfere with the intracellular replication of HIV, hepatitis B, HPV, and herpes virus. Additionally, CPAPs with activity against protozoa of the genera Leishmania, Trypanosoma, and Plasmodium, the etiological agents of Leishmaniasis, Chagas’ Disease, and Malaria, respectively. The information provided in this review emphasizes the potential of multivalent CPAPs, with anti-infective properties for application against various intracellular infections. So far, CPAPs bear a promise of druggability for the translational medical use of CPPs alone or in combination with chemotherapeutics. Moreover, CPAPs could be an exciting alternative for pharmaceutical design and treating intracellular infectious diseases. Full article
(This article belongs to the Special Issue The Century-Long Journey of Peptide-Based Drugs)
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