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Proteases: Structure and Drug Development
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Proteases: Structure and Drug Development

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

Deadline for manuscript submissions: closed (15 June 2021) | Viewed by 7358

Special Issue Editors

Prof. Dr. Steven Verhelst

E-Mail Website
Guest Editor
Laboratory of Chemical Biology, Department of Cellular and Molecular Medicine, KU Leuven, Belgium
Interests: activity-based probes; activity-based protein profiling; bioorthogonal chemistry; chemical proteomics; cleavable linkers; intramembrane proteases; photoaffinity labeling; proteases; protease inhibitors
Special Issues, Collections and Topics in MDPI journals
Prof. Dr. Joel D. A. Tyndall

E-Mail Website
Guest Editor
School of Pharmacy, University of Otago, Dunedin, New Zealand
Interests: drug design; modelling; CYP450; proteases; GPCRs; docking; infectious disease; drug targets; protein structure

Special Issue Information

Dear Colleagues,

Proteases (also called peptidases or proteinases) catalyze the breakdown of proteins into polypeptides or single amino acids. Proteases play an important role in many physiological functions from food digestion to signalling pathways. Tight regulation of protease activity is important for homeostasis, and a dysregulation can lead to many human diseases. Proteases are known drug targets with small molecule inhibitors currently used clinically against cancer and several viral targets.

This Special Issue welcomes the submission of original research, communications, and review manuscripts focusing on proteases as targets for diagnosis and therapy, inhibitor design, and discovery as well as structural characterization of medically relevant proteases.

Prof. Dr. Steven Verhelst
Prof. Dr. Joel D. A. Tyndall
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. 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

  • proteases
  • proteolysis
  • protease inhibitor
  • drug discovery
  • diagnostics

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Published Papers (2 papers)

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Research

13 pages, 2221 KiB  
Article
Discrimination of Methionine Sulfoxide and Sulfone by Human Neutrophil Elastase
by Darren Leahy, Cameron Grant, Alex Jackson, Alex Duff, Nicholas Tardiota, Jessica Van Haeften, Xingchen Chen, Jonathan M. Peake, Michael D. Kruppa, Eliot T. Smith, David A. Johnson, William B. Lott and Jonathan M. Harris
Molecules 2021, 26(17), 5344; https://doi.org/10.3390/molecules26175344 - 2 Sep 2021
Cited by 1 | Viewed by 2954
Abstract
Human neutrophil elastase (HNE) is a uniquely destructive serine protease with the ability to unleash a wave of proteolytic activity by destroying the inhibitors of other proteases. Although this phenomenon forms an important part of the innate immune response to invading pathogens, it [...] Read more.
Human neutrophil elastase (HNE) is a uniquely destructive serine protease with the ability to unleash a wave of proteolytic activity by destroying the inhibitors of other proteases. Although this phenomenon forms an important part of the innate immune response to invading pathogens, it is responsible for the collateral host tissue damage observed in chronic conditions such as chronic obstructive pulmonary disease (COPD), and in more acute disorders such as the lung injuries associated with COVID-19 infection. Previously, a combinatorially selected activity-based probe revealed an unexpected substrate preference for oxidised methionine, which suggests a link to oxidative pathogen clearance by neutrophils. Here we use oxidised model substrates and inhibitors to confirm this observation and to show that neutrophil elastase is specifically selective for the di-oxygenated methionine sulfone rather than the mono-oxygenated methionine sulfoxide. We also posit a critical role for ordered solvent in the mechanism of HNE discrimination between the two oxidised forms methionine residue. Preference for the sulfone form of oxidised methionine is especially significant. While both host and pathogens have the ability to reduce methionine sulfoxide back to methionine, a biological pathway to reduce methionine sulfone is not known. Taken together, these data suggest that the oxidative activity of neutrophils may create rapidly cleaved elastase “super substrates” that directly damage tissue, while initiating a cycle of neutrophil oxidation that increases elastase tissue damage and further neutrophil recruitment. Full article
(This article belongs to the Special Issue Proteases: Structure and Drug Development)
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19 pages, 3846 KiB  
Article
Functional Mining of the Crotalus Spp. Venom Protease Repertoire Reveals Potential for Chronic Wound Therapeutics
by David Meléndez-Martínez, Luis Fernando Plenge-Tellechea, Ana Gatica-Colima, Martha Sandra Cruz-Pérez, José Manuel Aguilar-Yáñez and Cuauhtémoc Licona-Cassani
Molecules 2020, 25(15), 3401; https://doi.org/10.3390/molecules25153401 - 28 Jul 2020
Cited by 10 | Viewed by 3713
Abstract
Chronic wounds are a major health problem that cause millions of dollars in expenses every year. Among all the treatments used, active wound treatments such as enzymatic treatments represent a cheaper and specific option with a fast growth category in the market. In [...] Read more.
Chronic wounds are a major health problem that cause millions of dollars in expenses every year. Among all the treatments used, active wound treatments such as enzymatic treatments represent a cheaper and specific option with a fast growth category in the market. In particular, bacterial and plant proteases have been employed due to their homology to human proteases, which drive the normal wound healing process. However, the use of these proteases has demonstrated results with low reproducibility. Therefore, alternative sources of proteases such as snake venom have been proposed. Here, we performed a functional mining of proteases from rattlesnakes (Crotalus ornatus, C. molossus nigrescens, C. scutulatus, and C. atrox) due to their high protease predominance and similarity to native proteases. To characterize Crotalus spp. Proteases, we performed different protease assays to measure and confirm the presence of metalloproteases and serine proteases, such as the universal protease assay and zymography, using several substrates such as gelatin, casein, hemoglobin, L-TAME, fibrinogen, and fibrin. We found that all our venom extracts degraded casein, gelatin, L-TAME, fibrinogen, and fibrin, but not hemoglobin. Crotalus ornatus and C. m. nigrescens extracts were the most proteolytic venoms among the samples. Particularly, C. ornatus predominantly possessed low molecular weight proteases (P-I metalloproteases). Our results demonstrated the presence of metalloproteases capable of degrading gelatin (a collagen derivative) and fibrin clots, whereas serine proteases were capable of degrading fibrinogen-generating fibrin clots, mimicking thrombin activity. Moreover, we demonstrated that Crotalus spp. are a valuable source of proteases that can aid chronic wound-healing treatments. Full article
(This article belongs to the Special Issue Proteases: Structure and Drug Development)
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