molecules-logo

Journal Browser

Journal Browser

The Chemical Immobilization and Inactivation of SARS-CoV-2

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

Deadline for manuscript submissions: closed (31 July 2024) | Viewed by 1072

Special Issue Editor


E-Mail Website
Guest Editor
Department of Bioactive Compounds, Faculty of Chemistry, Adam Mickiewicz University, Uniwersytetu Poznańskiego 8, 61-614 Poznan, Poland
Interests: organic synthesis; molecular interactions; surface chemistry; microbiocide chemistry; smart materials; corrosion inhibition; environmental chemistry
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

The outbreak and spread of SARS-CoV-2 is a serious global threat, unpredictable in its health, economic, and political effects. Tragic consequences of coronavirus infection will be mitigated in the future by vaccines and drugs. It will certainly take a long time. Faster extinction of the pandemic is possible by limiting the proliferation of the virus. Preventing the virus from contacting the host can be achieved by maintaining social distance, disinfection, and the use of materials which immobilize and inactivate viruses.

The surface of SARS-CoV-2 is covered by glycosylated S proteins, which are crucial to the viral life cycle. Therefore, these proteins are potential targets for active substances that can effectively immobilize and inactivate the virus. The formation of covalent or ionic bonds, sequestration, and intermolecular interactions play a fundamental role in the immobilization and inactivation of viruses. The introduction of bioactive substances to natural or synthetic polymers (PP, PLA, PANI, NNMO cellulose, chitosan) by electrospinning, melt-blowing, or other techniques will make it possible to obtain construction materials for protective clothing, masks, curtains, packaging materials, and protective layers forming a barrier to the virus.

The present Special Issue aims to provide an update on the synthesis of stable antiviral agents and their implementation in polymers to get bioactive materials which will limit the proliferation of SARS-CoV-2.

Prof. Dr. Bogumil E. Brycki
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. Molecules is an international peer-reviewed open access semimonthly 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 2700 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

  • antiviral agents
  • biocidal nanoparticles
  • mechanism of immobilization
  • antiviral activity
  • bioactive polymers
  • molecular docking
  • applications

Benefits of Publishing in a Special Issue

  • Ease of navigation: Grouping papers by topic helps scholars navigate broad scope journals more efficiently.
  • Greater discoverability: Special Issues support the reach and impact of scientific research. Articles in Special Issues are more discoverable and cited more frequently.
  • Expansion of research network: Special Issues facilitate connections among authors, fostering scientific collaborations.
  • External promotion: Articles in Special Issues are often promoted through the journal's social media, increasing their visibility.
  • e-Book format: Special Issues with more than 10 articles can be published as dedicated e-books, ensuring wide and rapid dissemination.

Further information on MDPI's Special Issue polices can be found here.

Published Papers (1 paper)

Order results
Result details
Select all
Export citation of selected articles as:

Research

13 pages, 2130 KiB  
Article
The Proteolytic Activity of Neutrophil-Derived Serine Proteases Bound to the Cell Surface Arming Lung Epithelial Cells for Viral Defense
by Akmaral Assylbekova, Maiya Allayarova, Moldir Konysbekova, Amanbek Bekturgan, Aiya Makhanova, Samantha Brown, Norbert Grzegorzek, Hubert Kalbacher, Ruslan Kalendar and Timo Burster
Molecules 2024, 29(18), 4449; https://doi.org/10.3390/molecules29184449 - 19 Sep 2024
Viewed by 320
Abstract
The collaboration between cellular proteases and host cells is pivotal in mounting an effective innate immune defense. Of particular interest is the synergistic interaction between cathepsin G (CatG) and neutrophil elastase (NE), which are proteases secreted by activated neutrophils, and the human alveolar [...] Read more.
The collaboration between cellular proteases and host cells is pivotal in mounting an effective innate immune defense. Of particular interest is the synergistic interaction between cathepsin G (CatG) and neutrophil elastase (NE), which are proteases secreted by activated neutrophils, and the human alveolar basal epithelial cell line (A549) and the human lung epithelial-like cell line (H1299), because of the potential implications for viral infection. Our study aimed to investigate the binding capacity of CatG and NE on the surface of A549 and H1299 cells through preincubation with purified CatG and NE; thereby, the proteolytic activity could be detected using activity-based probes. Both CatG and NE were capable of binding to the cell surface and exhibited proteolytic activity, leading to increased cell surface levels of MHC I molecules, which is crucial for displaying the endogenous antigenic repertoire. In addition, CatG cleaved the S2′ site of the SARS-CoV-2 spike protein at two specific sites (815RS816 and 817FI818) as well as NE (813SK814 and 818IE819), which potentially leads to the destruction of the fusion peptide. Additionally, furin required the presence of Ca2+ ions for the distinct cleavage site necessary to generate the fusion peptide. Overall, the findings suggest that CatG and NE can fortify target cells against viral entry, underscoring the potential significance of cell surface proteases in protecting against viral invasion. Full article
(This article belongs to the Special Issue The Chemical Immobilization and Inactivation of SARS-CoV-2)
Show Figures

Graphical abstract

Back to TopTop