Vaccines and Antivirals against Emerging Viruses

A special issue of Biomedicines (ISSN 2227-9059). This special issue belongs to the section "Molecular and Translational Medicine".

Deadline for manuscript submissions: closed (31 January 2024) | Viewed by 2105

Special Issue Editor


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Guest Editor
Department of Molecular and Cell Biology, National Center of Biotechnology (CNB-CSIC), Campus Universidad Autónoma de Madrid, Darwin 3, 28049 Madrid, Spain
Interests: coronaviruses; antivirals; pathogenesis; vaccines

Special Issue Information

Dear Colleagues,

A viral disease is considered emerging when it is caused by a novel virus, when it appears for the first time in a specific population, or when the incidence of a known pathogen increases locally or is extended to other local areas. In recent decades many novel infectious diseases have been identified as having been caused by emerging viruses, most of them due to zoonosis. These viruses have been high repercussion in global health, even leading to pandemics, such as the recent example of SARS-CoV-2.

In this Special Issue of Vaccines and Antivirals against emerging viruses, we seek research papers contributing to show novel or existing compounds and strategies with potential to prevent or treat viral diseases. In addition, we are interested in papers that describe potential targets to develop antivirals and the molecular methods for diagnosis.

Dr. Melissa Belló-Pérez
Guest Editor

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Keywords

  • viruses
  • vaccines
  • antivirals
  • reservoirs
  • pandemics
  • pathogenesis
  • virulence
  • antibodies
  • emerging infectious diseases
  • antiviral immunity

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Published Papers (1 paper)

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Research

19 pages, 3397 KiB  
Article
Solid Phase Synthesis and TAR RNA-Binding Activity of Nucleopeptides Containing Nucleobases Linked to the Side Chains via 1,4-Linked-1,2,3-triazole
by Piotr Mucha, Małgorzata Pieszko, Irena Bylińska, Wiesław Wiczk, Jarosław Ruczyński, Katarzyna Prochera and Piotr Rekowski
Biomedicines 2024, 12(3), 570; https://doi.org/10.3390/biomedicines12030570 - 3 Mar 2024
Cited by 1 | Viewed by 1670
Abstract
Nucleopeptides (NPs) represent synthetic polymers created by attaching nucleobases to the side chains of amino acid residues within peptides. These compounds amalgamate the characteristics of peptides and nucleic acids, showcasing a unique ability to recognize RNA structures. In this study, we present the [...] Read more.
Nucleopeptides (NPs) represent synthetic polymers created by attaching nucleobases to the side chains of amino acid residues within peptides. These compounds amalgamate the characteristics of peptides and nucleic acids, showcasing a unique ability to recognize RNA structures. In this study, we present the design and synthesis of Fmoc-protected nucleobase amino acids (1,4-TzlNBAs) and a new class of NPs, where canonical nucleobases are affixed to the side chain of L-homoalanine (Hal) through a 1,4-linked-1,2,3-triazole (HalTzl). Fmoc-protected 1,4-TzlNBAs suitable for HalTzl synthesis were obtained via Cu(I)-catalyzed azide–alkyne cycloaddition (CuAAC) conjugation of Fmoc-L-azidohomoalanine (Fmoc-Aha) and N1- or N9-propargylated nucleobases or their derivatives. Following this, two trinucleopeptides, HalTzlAAA and HalTzlAGA, and the hexanucleopeptide HalTzlTCCCAG, designed to complement bulge and outer loop structures of TAR (trans-activation response element) RNA HIV-1, were synthesized using the classical solid-phase peptide synthesis (SPPS) protocol. The binding between HalTzls and fluorescently labeled 5′-(FAM(6))-TAR UCU and UUU mutant was characterized using circular dichroism (CD) and fluorescence spectroscopy. CD results confirmed the binding of HalTzls to TAR RNA, which was evident by a decrease in ellipticity band intensity around 265 nm during complexation. CD thermal denaturation studies indicated a relatively modest effect of complexation on the stability of TAR RNA structure. The binding of HalTzls at an equimolar ratio only marginally increased the melting temperature (Tm) of the TAR RNA structure, with an increment of less than 2 °C in most cases. Fluorescence spectroscopy revealed that HalTzlAAA and HalTzlAGA, complementary to UUU or UCU bulges, respectively, exhibited disparate affinities for the TAR RNA structure (with Kd ≈ 30 and 256 µM, respectively). Hexamer HalTzlTCCCAG, binding to the outer loop of TARUCU, demonstrated a moderate affinity with Kd ≈ 38 µM. This study demonstrates that newly designed HalTzls effectively bind the TAR RNA structure, presenting a potential new class of RNA binders and may be a promising scaffold for the development of a new class of antiviral drugs. Full article
(This article belongs to the Special Issue Vaccines and Antivirals against Emerging Viruses)
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