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Biomedicines
Special Issues
Amino Acid and Peptide Synthesis
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Amino Acid and Peptide Synthesis

A special issue of Biomedicines (ISSN 2227-9059). This special issue belongs to the section "Drug Discovery, Development and Delivery".

Deadline for manuscript submissions: closed (30 November 2020) | Viewed by 9926

Special Issue Editors

Prof. Angelo Liguori

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Guest Editor
Department of Pharmacy, Health and Nutritional Sciences, University of Calabria, Rende (CS), Italy
Interests: peptide synthesis; modified amino acids; modified peptides; N-methylated amino acids; N-methylated peptides; anticancer peptides; Lewis acid mediated reactions; mass spectrometry
Special Issues, Collections and Topics in MDPI journals
Prof. Antonella Leggio

E-Mail Website1 Website2
Guest Editor
Department of Pharmacy, Health and Nutritional Sciences, University of Calabria, Rende (CS), Italy
Interests: peptide synthesis; modified amino acids; modified peptides; N-methylated amino acids; N-methylated peptides; anticancer peptides; Lewis acid mediated reactions; mass spectrometry; nanostructured drug delivery systems
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

This Special Issue presents the latest developments in amino acid and peptide synthesis. Peptides control a wide range of physiological processes, and interact with the biological targets involved in different pathologies, thus providing a vast opportunity for biomedical applications. Recently, biologically active peptides and their therapeutic potential have aroused growing interest in the pharmaceutical industry, which has resulted in the marketing of numerous peptide drugs, many of which are in clinical trials. Peptide drugs have high specificity and selectivity, combined with low toxicity; therefore, they represent an excellent starting point for the design of new therapies. However, the biomedical application of peptide-based drugs can be restricted by their low proteolytic stability and poor bioavailability. This has led to the design and development of bioactive peptide analogs containing suitable chemical modifications that can increase their bioactivity and biodistribution.

Original research articles and review articles covering all areas of peptide synthesis, with a particular emphasis on the synthesis of modified amino acids and peptides are welcome in this Special Issue, so as to provide readers with novel insights into the synthetic strategies in this interesting research area.

This Special Issue is jointly organized between IJMS and Biomedicines. According to the aims and scopes of these journals, articles showing basic studies in biochemistry, molecular biology, and molecular medicine can be submitted to IJMS, while articles presenting a more clinical content can be submitted to Biomedicines.

Prof. Angelo Liguori
Prof. Antonella Leggio
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. Biomedicines 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 2600 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

  • solid-phase peptide synthesis
  • solution-phase peptide synthesis
  • coupling agents
  • protecting groups
  • modified amino acids
  • modified peptides
  • peptidomimetics

Published Papers (3 papers)

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Research

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17 pages, 2973 KiB  
Article
NHS-Functionalized THP Derivative for Efficient Synthesis of Kit-Based Precursors for 68Ga Labeled PET Probes
by Giuseppe Floresta, George P. Keeling, Siham Memdouh, Levente K. Meszaros, Rafael T. M. de Rosales and Vincenzo Abbate
Biomedicines 2021, 9(4), 367; https://doi.org/10.3390/biomedicines9040367 - 1 Apr 2021
Cited by 8 | Viewed by 3045
Abstract
Hexadentate tris(3,4-hydroxypyridinone) ligands (THP) complex Fe3+ at very low iron concentrations and their high affinities for oxophilic trivalent metal ions have led to their development for new applications as bifunctional chelators for the radiometal gallium-68 (68Ga). THP-peptide bioconjugates rapidly and [...] Read more.
Hexadentate tris(3,4-hydroxypyridinone) ligands (THP) complex Fe3+ at very low iron concentrations and their high affinities for oxophilic trivalent metal ions have led to their development for new applications as bifunctional chelators for the radiometal gallium-68 (68Ga). THP-peptide bioconjugates rapidly and quantitatively complex 68Ga at room temperature, neutral pH, and micromolar ligand concentrations, making them amenable to kit-based radiosynthesis of 68Ga PET radiopharmaceuticals. With the aim to produce an N-hydroxysuccinimide-(NHS)-THP reagent for kit-based 68Ga-labeling and PET imaging, THP-derivatives were designed and synthesized to exploit the advantages of NHS chemistry for coupling with peptides, proteins, and antibodies. The more stable five-carbon atoms linker product was selected for a proof-of-concept conjugation and radiolabeling study with an anti-programmed death ligand 1 (PD-L1) camelid single domain antibody (sdAb) under mild conditions and further evaluated for site-specific amide bond formation with a synthesized glucagon-like peptide-1 (GLP-1) targeting peptide using solid-phase synthesis. The obtained THP-GLP-1 conjugate was tested for its 68Ga chelating ability, demonstrating to be a promising candidate for the detection and monitoring of GLP-1 aberrant malignancies. The obtained sdAb-THP conjugate was radiolabeled with 68Ga under mild conditions, providing sufficient labeling yields after 5 min, demonstrating that the novel NHS-THP bifunctional chelator can be widely used to easily conjugate the THP moiety to different targeting molecules (e.g., antibodies, anticalins, or peptides) under mild conditions, paving the way to the synthesis of different imaging probes with all the advantages of THP radiochemistry. Full article
(This article belongs to the Special Issue Amino Acid and Peptide Synthesis)
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19 pages, 2426 KiB  
Article
Searching for Peptide Inhibitors of T Regulatory Cell Activity by Targeting Specific Domains of FOXP3 Transcription Factor
by Teresa Lozano, Noelia Casares, Celia Martil-Otal, Blanca Anega, Marta Gorraiz, Jonathan Parker, Marta Ruiz, Virginia Belsúe, Antonio Pineda-Lucena, Julen Oyarzabal and Juan José Lasarte
Biomedicines 2021, 9(2), 197; https://doi.org/10.3390/biomedicines9020197 - 17 Feb 2021
Cited by 4 | Viewed by 3192
Abstract
(1) Background: The ability of cancer cells to evade the immune system is due in part to their capacity to induce and recruit T regulatory cells (Tregs) to the tumor microenvironment. Strategies proposed to improve antitumor immunity by depleting Tregs generally lack specificity [...] Read more.
(1) Background: The ability of cancer cells to evade the immune system is due in part to their capacity to induce and recruit T regulatory cells (Tregs) to the tumor microenvironment. Strategies proposed to improve antitumor immunity by depleting Tregs generally lack specificity and raise the possibility of autoimmunity. Therefore, we propose to control Tregs by their functional inactivation rather than depletion. Tregs are characterized by the expression of the Forkhead box protein 3 (FOXP3) transcription factor, which is considered their “master regulator”. Its interaction with DNA is assisted primarily by its interaction with other proteins in the so-called “Foxp3 interactome”, which elicits much of the characteristic Treg cell transcriptional signature. We speculated that the disruption of such a protein complex by using synthetic peptides able to bind Foxp3 might have an impact on the functionality of Treg cells and thus have a therapeutic potential in cancer treatment. (2) Methods: By using a phage-displayed peptide library, or short synthetic peptides encompassing Foxp3 fragments, or by studying the crystal structure of the Foxp3:NFAT complex, we have identified a series of peptides that are able to bind Foxp3 and inhibit Treg activity. (3) Results: We identified some peptides encompassing fragments of the leuzin zipper or the C terminal domain of Foxp3 with the capacity to inhibit Treg activity in vitro. The acetylation/amidation of linear peptides, head-to-tail cyclization, the incorporation of non-natural aminoacids, or the incorporation of cell-penetrating peptide motifs increased in some cases the Foxp3 binding capacity and Treg inhibitory activity of the identified peptides. Some of them have shown antitumoral activity in vivo. (4) Conclusions: Synthetic peptides constitute an alternative to inhibit Foxp3 protein–protein interactions intracellularly and impair Treg immunosuppressive activity. These peptides might be considered as potential hit compounds on the design of new immunotherapeutic approaches against cancer. Full article
(This article belongs to the Special Issue Amino Acid and Peptide Synthesis)
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Review

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21 pages, 4072 KiB  
Review
Well-Defined Construction of Functional Macromolecular Architectures Based on Polymerization of Amino Acid Urethanes
by Takeshi Endo and Atsushi Sudo
Biomedicines 2020, 8(9), 317; https://doi.org/10.3390/biomedicines8090317 - 29 Aug 2020
Cited by 4 | Viewed by 3142
Abstract
Polypeptide synthesis was accomplished using the urethane derivatives of amino acids as monomers, which can be easily prepared, purified, and stored at ambient temperature without the requirement for special precautions. The urethanes of amino acids are readily synthesized by the N-carbamoylation of [...] Read more.
Polypeptide synthesis was accomplished using the urethane derivatives of amino acids as monomers, which can be easily prepared, purified, and stored at ambient temperature without the requirement for special precautions. The urethanes of amino acids are readily synthesized by the N-carbamoylation of onium salts of amino acids using diphenyl carbonate (DPC). The prepared urethanes are then efficiently cyclized to produce amino acid N-carboxyanhydrides (NCAs). Thereafter, in the presence of primary amines, the ring-opening polymerization (ROP) of NCAs is initiated using the amines, to yield polypeptides with controlled molecular weights. The polypeptides have propagating chains bearing reactive amino groups and initiating chain ends endowed with functional moieties that originate from the amines. Aiming to benefit from these interesting characteristics of the polypeptide synthesis using the urethanes of amino acids, various macromolecular architectures containing polypeptide components have been constructed and applied as biofunctional materials in highly efficient antifouling coatings against proteins and cells, as biosensors for specific molecules, and in targeted drug delivery. Full article
(This article belongs to the Special Issue Amino Acid and Peptide Synthesis)
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