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Special Issue "Metalloenzyme Inhibitors and Activators"

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

Deadline for manuscript submissions: 28 February 2018

Special Issue Editor

Guest Editor
Prof. Dr. Claudiu T. Supuran

Neurofarba Department, Sezione di Scienze Farmaceutiche e Nutraceutiche, Università degli Studi di Firenze, Sesto Fiorentino (Florence) 50019, Italy
Website | E-Mail
Phone: +39-055-4573729/3005
Fax: +39-055-4573385
Interests: drug design; metalloenzymes; carbonic anhydrases; anticancer agents; antiinfectives; sulfonamides; coumarins

Special Issue Information

Dear Colleagues,

Enzymes have long been considered as important drug targets for the treatment of major human diseases, as several thousands of such proteins are encoded in the human genome, and they play key roles in virtually every physiological/pathological process. Currently, at least 70 human enzymes and 20 bacterial, viral, fungal or parasite enzymes are targets of approved drugs, e.g., up to 40% of the current known drug targets. Enzymes containing metals (metalloenzymes) are of increasing interest and importance, as the genetic and phsysiologic consequences of metalloprotein regulation became better understood processes. All major six enzyme classes established by the International Union of Biochemistry, i.e., oxidoreductases, transferases, hydrolases, lyases, isomerases and ligases have important members among the metalloenzymes known to date. Over the last years, important achievements have been done regarding their characterization, with crucial inhibition/activation studies which led to the identifications of compounds with potential pharmacologic and biotechnologic applications. The present Special Issue of Molecules welcomes contributions dealing with all aspects of metalloenzymes research, including drug design, inhibitors, activators, structure–function relationship, etc.

Prof. Dr. Claudiu T. Supuran
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 papers will be 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 monthly 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 1800 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

  • metalloenzyme
  • enzyme inhibitor
  • enzyme activator
  • structure-function relationship
  • drug design
  • metal-binding function

Published Papers (2 papers)

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Research

Open AccessArticle Development of a Non-Hydroxamate Dual Matrix Metalloproteinase (MMP)-7/-13 Inhibitor
Molecules 2017, 22(9), 1548; doi:10.3390/molecules22091548
Received: 26 August 2017 / Revised: 8 September 2017 / Accepted: 8 September 2017 / Published: 14 September 2017
PDF Full-text (3258 KB) | HTML Full-text | XML Full-text | Supplementary Files
Abstract
Matrix metalloproteinase 7 (MMP-7) is a member of the MMP superfamily and is able to degrade extracellular matrix proteins such as casein, gelatin, fibronectin and proteoglycan. MMP-7 is a validated target for the development of small molecule drugs against cancer. MMP-13 is within
[...] Read more.
Matrix metalloproteinase 7 (MMP-7) is a member of the MMP superfamily and is able to degrade extracellular matrix proteins such as casein, gelatin, fibronectin and proteoglycan. MMP-7 is a validated target for the development of small molecule drugs against cancer. MMP-13 is within the enzyme class the most efficient contributor to type II collagen degeneration and is a validated target in arthritis and cancer. We have developed the dual MMP-7/-13 inhibitor ZHAWOC6941 with IC50-values of 2.2 μM (MMP-7) and 1.2 μM (MMP-13) that is selective over a broad range of MMP isoforms. It spares MMP-1, -2, -3, -8, -9, -12 and -14, making it a valuable modulator for targeted polypharmacology approaches. Full article
(This article belongs to the Special Issue Metalloenzyme Inhibitors and Activators)
Figures

Open AccessArticle Anti-Melanogenic Effects of Flavonoid Glycosides from Limonium tetragonum (Thunb.) Bullock via Inhibition of Tyrosinase and Tyrosinase-Related Proteins
Molecules 2017, 22(9), 1480; doi:10.3390/molecules22091480
Received: 20 July 2017 / Revised: 30 August 2017 / Accepted: 2 September 2017 / Published: 5 September 2017
PDF Full-text (1593 KB) | HTML Full-text | XML Full-text
Abstract
Overproduction and stimulation of tyrosinase result in increased melanogenesis of which several skin disorders such as freckles, spots, and hyperpigmentation appear as complications. Limonium tetragonum is a halophyte well-known for its antioxidative properties. This study investigated the anti-melanogenic effects of solvent-partitioned L. tetragonum
[...] Read more.
Overproduction and stimulation of tyrosinase result in increased melanogenesis of which several skin disorders such as freckles, spots, and hyperpigmentation appear as complications. Limonium tetragonum is a halophyte well-known for its antioxidative properties. This study investigated the anti-melanogenic effects of solvent-partitioned L. tetragonum extracts (LTEs) and its bioactive constituents, two isolated flavonoid glycosides. Current study followed a set of experiments on B16-F10 mouse melanoma cell model with a focus on tyrosinase activity and production. The anti-melanogenic capacity of LTEs was confirmed by their tyrosinase inhibitory effects, prevention of DOPA oxidation, and suppression of melanin production. The inhibition of tyrosinase and DOPA oxidation by LTEs was suggested to be related with the downregulation of microphthalmia-associated transcription factor, tyrosinase, tyrosinase-related protein-1, and tyrosinase-related protein-2, verified with mRNA and protein expression levels. Among all tested LTEs, 85% aq. MeOH and n-BuOH were found to be the most active fractions which later yielded the two known compounds, myricetin 3-galactoside and quercetin 3-O-β-galactopyronaside. The anti-melanogenic potential of the compounds were confirmed by their tyrosinase inhibitory effects. These results suggested that L. tetragonum may serve as a potential source of bioactive substances with effective anti-melanogenesis properties. Full article
(This article belongs to the Special Issue Metalloenzyme Inhibitors and Activators)
Figures

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