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Amino Acid and Peptide Synthesis
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Amino Acid and Peptide Synthesis

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: closed (30 November 2020) | Viewed by 16356

Special Issue Editors

Prof. Angelo Liguori

E-Mail Website
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 is aimed to present 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 a high specificity and selectivity, combined with a 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 analogues containing suitable chemical modifications able to 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 welcomed 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. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. 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

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Published Papers (3 papers)

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Research

14 pages, 1665 KiB  
Article
Solid-Phase Synthesis and In-Silico Analysis of Iron-Binding Catecholato Chelators
by Ranko Gacesa, Andrea A. P. Tripodi, Agostino Cilibrizzi, Antonella Leggio, Robert Hider and Vincenzo Abbate
Int. J. Mol. Sci. 2020, 21(20), 7498; https://doi.org/10.3390/ijms21207498 - 12 Oct 2020
Cited by 1 | Viewed by 3248
Abstract
Siderophores are iron-complexing compounds synthesized by bacteria and fungi. They are low molecular weight compounds (500-1500 Daltons) possessing high affinity for iron(III). Since 1970 a large number of siderophores have been characterized, the majority using hydroxamate or catecholate as functional groups. The biosynthesis [...] Read more.
Siderophores are iron-complexing compounds synthesized by bacteria and fungi. They are low molecular weight compounds (500-1500 Daltons) possessing high affinity for iron(III). Since 1970 a large number of siderophores have been characterized, the majority using hydroxamate or catecholate as functional groups. The biosynthesis of siderophores is typically regulated by the iron levels of the environment where the organism is located. Because of their exclusive affinity and specificity for iron(III), natural siderophores and their synthetic derivatives have been exploited in the treatment of human iron-overload diseases, as both diagnostic and therapeutic agents. Here, solid-phase approach for the preparation of hexadentate, peptide-based tricatecholato containing peptides is described. The versatility of the synthetic method allows for the design of a common scaffolding structure whereby diverse ligands can be conjugated. With so many possibilities, a computational approach has been developed which will facilitate the identification of those peptides which are capable of providing a high affinity iron(III) binding site. This study reports an integrated computational/synthetic approach towards a rational development of peptide-based siderophores. Full article
(This article belongs to the Special Issue Amino Acid and Peptide Synthesis)
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22 pages, 7831 KiB  
Article
Biosynthesized Multivalent Lacritin Peptides Stimulate Exosome Production in Human Corneal Epithelium
by Changrim Lee, Maria C. Edman, Gordon W. Laurie, Sarah F. Hamm-Alvarez and J. Andrew MacKay
Int. J. Mol. Sci. 2020, 21(17), 6157; https://doi.org/10.3390/ijms21176157 - 26 Aug 2020
Cited by 10 | Viewed by 4371
Abstract
Lacripep is a therapeutic peptide derived from the human tear protein, Lacritin. Lacripep interacts with syndecan-1 and induces mitogenesis upon the removal of heparan sulfates (HS) that are attached at the extracellular domain of syndecan-1. The presence of HS is a prerequisite for [...] Read more.
Lacripep is a therapeutic peptide derived from the human tear protein, Lacritin. Lacripep interacts with syndecan-1 and induces mitogenesis upon the removal of heparan sulfates (HS) that are attached at the extracellular domain of syndecan-1. The presence of HS is a prerequisite for the syndecan-1 clustering that stimulates exosome biogenesis and release. Therefore, syndecan-1-mediated mitogenesis versus HS-mediated exosome biogenesis are assumed to be mutually exclusive. This study introduces a biosynthesized fusion between Lacripep and an elastin-like polypeptide named LP-A96, and evaluates its activity on cell motility enhancement versus exosome biogenesis. LP-A96 activates both downstream pathways in a dose-dependent manner. HCE-T cells at high confluence treated with 1 μM LP-A96 enhanced cell motility equipotent to Lacripep. However, cells at low density treated with 1 μM LP-A96 generated a 210-fold higher number of exosomes compared to those treated at low density with Lacripep. As monovalent Lacripep is capable of enhancing cell motility but not exosome biogenesis, activation of exosome biogenesis by LP-A96 not only suggests its utility as a novel molecular tool to study the Lacritin biology in the corneal epithelium but also implies activity as a potential therapeutic peptide that can further improve ocular surface health through the induction of exosomes. Full article
(This article belongs to the Special Issue Amino Acid and Peptide Synthesis)
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12 pages, 1839 KiB  
Article
Revisiting NO2 as Protecting Group of Arginine in Solid-Phase Peptide Synthesis
by Mahama Alhassan, Ashish Kumar, John Lopez, Fernando Albericio and Beatriz G. de la Torre
Int. J. Mol. Sci. 2020, 21(12), 4464; https://doi.org/10.3390/ijms21124464 - 23 Jun 2020
Cited by 8 | Viewed by 8055
Abstract
The protection of side-chain arginine in solid-phase peptide synthesis requires attention since current protecting groups have several drawbacks. Herein, the NO2 group, which is scarcely used, has been revisited. This work shows that it prevents the formation of δ-lactam, the most severe [...] Read more.
The protection of side-chain arginine in solid-phase peptide synthesis requires attention since current protecting groups have several drawbacks. Herein, the NO2 group, which is scarcely used, has been revisited. This work shows that it prevents the formation of δ-lactam, the most severe side-reaction during the incorporation of Arg. Moreover, it is stable in solution for long periods and can be removed in an easy-to-understand manner. Thus, this protecting group can be removed while the protected peptide is still anchored to the resin, with SnCl2 as reducing agent in mild acid conditions using 2-MeTHF as solvent at 55 °C. Furthermore, we demonstrate that sonochemistry can facilitate the removal of NO2 from multiple Arg-containing peptides. Full article
(This article belongs to the Special Issue Amino Acid and Peptide Synthesis)
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