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The Role of Peptides and Peptidomimetics in Drug Discovery

A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Medicinal Chemistry".

Deadline for manuscript submissions: 31 December 2024 | Viewed by 473

Special Issue Editor


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Guest Editor
Department of Cellular Biology & Pharmacology, Herbert Wertheim College of Medicine, Florida International University, Miami, FL 33199, USA
Interests: organic chemistry; medicinal chemistry; small molecules; drug-like compounds; tethered and fused diazacyclic compounds; heterocyclic peptidomimetics; combinatorial chemistry; solid phase organic synthesis
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Special Issue Information

Dear Colleagues,

Peptide and Peptidomimetic drug discovery has progressed tremendously over the last two decades to become an extraordinary field which has resulted in a substantial body of multidisciplinary research. It has engaged synthetic, computational, and biophysical chemists, biochemists, pharmacologists, and drug development scientists worldwide to create novel molecule lead compounds, clinical candidates, and breakthrough medicines. Immense efforts have been dedicated towards developing therapeutic entities that can modulate intracellular proteins. Molecules that can readily cross cell membranes are becoming a frequent need in biological research, drug discovery, and medicine. A wide variety of natural peptides and peptidomimetics have been obtained and studied, and many others are advancing through clinical trials, covering multiple therapeutic areas.

Taking advantage of the diversity within the amino acid functionalities and stereochemistry that are commercially available as standard Fmoc/Boc amino acids, as well as the benefits of solid phase peptide synthesis, various synthetic strategies have been developed over the years to modulate the conformational flexibility and the peptide character of peptidomimetic compounds. This Special Issue calls for papers to elucidate the most effective strategy for the synthesis of peptides, cyclic peptides, and peptidomimetics, and the use of such approaches in the identification of active therapeutics with peptide structures.

Prof. Dr. Adel Nefzi
Guest Editor

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Keywords

  • peptide synthesis
  • peptide therapeutics
  • cyclic peptides
  • peptidomimetics
  • peptide drug discovery
  • modified peptides
  • bioactive peptides

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Published Papers (2 papers)

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Research

21 pages, 1802 KiB  
Article
Peptide Dimerization as a Strategy for the Development of Antileishmanial Compounds
by Natália C. S. Coelho, Deivys L. F. Portuondo, Jhonatan Lima, Angela M. A. Velásquez, Valéria Valente, Iracilda Z. Carlos, Eduardo M. Cilli and Márcia A. S. Graminha
Molecules 2024, 29(21), 5170; https://doi.org/10.3390/molecules29215170 - 31 Oct 2024
Abstract
Leishmaniasis is recognized as a serious public health problem in Brazil and around the world. The limited availability of drugs for treatment, added to the diversity of side effects and the emergence of resistant strains, shows the importance of research focused on the [...] Read more.
Leishmaniasis is recognized as a serious public health problem in Brazil and around the world. The limited availability of drugs for treatment, added to the diversity of side effects and the emergence of resistant strains, shows the importance of research focused on the development of new molecules, thus contributing to treatments. Therefore, this work aimed to identify leishmanicidal compounds using a peptide dimerization strategy, as well as to understand their mechanisms of action. Herein, it was demonstrated that the dimerization of the peptide TSHa, (TSHa)2K, presented higher potency and selectivity than its monomeric form when evaluated against Leishmania mexicana and Leishmania amazonensis. Furthermore, these compounds are capable of inhibiting the parasite cysteine protease, an important target explored for the development of antileishmanial compounds, as well as to selectively interact with the parasite membranes, as demonstrated by flow cytometry, permeabilization, and fluorescence microscopy experiments. Based on this, the identified molecules are candidates for use in in vivo studies with animal models to combat leishmaniasis. Full article
(This article belongs to the Special Issue The Role of Peptides and Peptidomimetics in Drug Discovery)
13 pages, 609 KiB  
Article
The Inhibition of Serum Amyloid A Protein Aggregation by a Five-Residue Peptidomimetic: Structural and Morphological Insights
by Julia Witkowska, Sandra Skibiszewska, Paweł Wityk, Marcel Pilarski and Elżbieta Jankowska
Molecules 2024, 29(21), 5165; https://doi.org/10.3390/molecules29215165 - 31 Oct 2024
Abstract
Serum amyloid A (SAA) is a small protein consisting of 104 residues and, under physiological conditions, exists mainly in hexameric form. It belongs to the positive acute-phase proteins, which means that its plasma concentration increases rapidly in response to injury, inflammation, and infection. [...] Read more.
Serum amyloid A (SAA) is a small protein consisting of 104 residues and, under physiological conditions, exists mainly in hexameric form. It belongs to the positive acute-phase proteins, which means that its plasma concentration increases rapidly in response to injury, inflammation, and infection. The accumulation of SAA molecules promotes the formation of amyloid aggregates, which deposit extracellularly in many organs, causing their dysfunction. In our previous work, we successfully designed a peptidomimetic that inhibited the aggregation of amyloidogenic SAA fragments. In the present paper, we show how the same inhibitor, named saa3Dip, affects the oligomerization and aggregation processes of MetSAA1.1 protein. The thioflavin T assay showed that saa3Dip inhibited its fibrillization. The measurement of the internal fluorophore fluorescence (Trp) showed differences that occurred in the tertiary structure of MetSAA1.1 in the presence of the inhibitor, which was also confirmed by CD spectra in the aromatic range. FTIR results suggested that saa3Dip could stabilize some fragments of the native structure of MetSAA1.1, which was confirmed by determining the melting temperature (Tm) of the protein–inhibitor complex. AFM images demonstrated that the presence of saa3Dip prevented the formation of large SAA aggregates. Our results suggest that saa3Dip stabilizes the native conformation of MetSAA1.1. Full article
(This article belongs to the Special Issue The Role of Peptides and Peptidomimetics in Drug Discovery)
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