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Editorial Board Members’ Collection Series: “Bacterial Enzymes as Targets”

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

Deadline for manuscript submissions: 30 June 2024 | Viewed by 1191

Special Issue Editors


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Guest Editor
Institute of Bioscience and Bioresources (IBBR), National Research Council, Via Pietro Castellino 111, 80131 Napoli, Italy
Interests: protein biochemistry; recombinant protein; heterologous expression; carbonic anhydrase; enzyme and protein purification; enzyme characterization; enzyme thermostability; cold-adapted enzymes
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Guest Editor
Phage Therapy Center, University Center for Applied and Interdisciplinary Research, University of Gdansk, Gdansk, Poland
Interests: biology of bacteriophages; biodiversity of bacteriophages; regulation of bacteriophage development; regulation of phage gene expression; control of phage DNA replication; phage therapy; phages bearing genes of toxins; bacteriophage genomics
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Exploring the enzymes essential for key bacterial functions presents an opportunity to develop innovative strategies for combating bacterial infections. Enzymes involved in cell wall biosynthesis are critical for maintaining bacterial cell structure and integrity. By inhibiting these enzymes, it is possible to disrupt cell wall formation, rendering bacteria susceptible to immune responses or other treatments. Similarly, enzymes involved in DNA replication are essential for bacterial proliferation. Targeting these enzymes can impede DNA synthesis and disrupt bacterial replication, potentially curbing infection progression. Bacteria often harbor metabolic pathways distinct from those of human cells, presenting opportunities that allow bacterial enzymes to be selectively targeted without affecting host cells. Moreover, by focusing on enzymes pivotal for bacterial survival, such as carbonic anhydrase, novel therapeutic strategies can be designed to offer effective treatment options for bacterial infections. Thus, the process of understanding and targeting specific bacterial enzymes represents a promising avenue for the development of novel antibacterial agents, as well as for tackling infections and combating antibiotic resistance.

Prof. Dr. Clemente Capasso
Prof. Dr. Alicja Wegrzyn
Guest Editors

Manuscript Submission Information

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Keywords

  • enzymes
  • cell wall biosynthesis
  • DNA replication
  • metabolic pathway
  • vital bacterial function
  • enzyme inhibition
  • antibacterial agents
  • antibiotic resistance

Published Papers (1 paper)

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Research

13 pages, 2862 KiB  
Article
Benzothiadiazinone-1,1-Dioxide Carbonic Anhydrase Inhibitors Suppress the Growth of Drug-Resistant Mycobacterium tuberculosis Strains
by Silvia Bua, Alessandro Bonardi, Georgiana Ramona Mük, Alessio Nocentini, Paola Gratteri and Claudiu T. Supuran
Int. J. Mol. Sci. 2024, 25(5), 2584; https://doi.org/10.3390/ijms25052584 - 23 Feb 2024
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Abstract
2H-Benzo[e][1,2,4]thiadiazin-3(4H)-one 1,1-dioxide (BTD) based carbonic anhydrase (CA) inhibitors are here explored as new anti-mycobacterial agents. The chemical features of BTD derivatives meet the criteria for a potent inhibition of β-class CA isozymes. BTD derivatives show chemical features meeting the [...] Read more.
2H-Benzo[e][1,2,4]thiadiazin-3(4H)-one 1,1-dioxide (BTD) based carbonic anhydrase (CA) inhibitors are here explored as new anti-mycobacterial agents. The chemical features of BTD derivatives meet the criteria for a potent inhibition of β-class CA isozymes. BTD derivatives show chemical features meeting the criteria for a potent inhibition of β-class CA isozymes. Specifically, three β-CAs (MtCA1, MtCA2, and MtCA3) were identified in Mycobacterium tuberculosis and their inhibition was shown to exert an antitubercular action. BTDs derivatives 2a-q effectively inhibited the mycobacterial CAs, especially MtCA2 and MtCA3, with Ki values up to a low nanomolar range (MtCA3, Ki = 15.1–2250 nM; MtCA2, Ki = 38.1–4480 nM) and with a significant selectivity ratio over the off-target human CAs I and II. A computational study was conducted to elucidate the compound structure-activity relationship. Importantly, the most potent MtCA inhibitors demonstrated efficacy in inhibiting the growth of M. tuberculosis strains resistant to both rifampicin and isoniazid—standard reference drugs for Tuberculosis treatment. Full article
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