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Novel Matrix Metalloproteinase-9 (MMP-9) Inhibitors in Cancer Treatment

Matrix metalloproteinases (MMPs) belong to a family of zinc-dependent proteolytic metalloenzymes. MMP-9, a member of the gelatinase B family, is characterized as one of the most intricate MMPs. The crucial involvement of MMP-9 in extracellular matrix (ECM) remodeling underscores its significant corr...

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Detalles Bibliográficos
Autores principales: Rashid, Zainab Ahmed, Bardaweel, Sanaa K.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10418771/
https://www.ncbi.nlm.nih.gov/pubmed/37569509
http://dx.doi.org/10.3390/ijms241512133
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author Rashid, Zainab Ahmed
Bardaweel, Sanaa K.
author_facet Rashid, Zainab Ahmed
Bardaweel, Sanaa K.
author_sort Rashid, Zainab Ahmed
collection PubMed
description Matrix metalloproteinases (MMPs) belong to a family of zinc-dependent proteolytic metalloenzymes. MMP-9, a member of the gelatinase B family, is characterized as one of the most intricate MMPs. The crucial involvement of MMP-9 in extracellular matrix (ECM) remodeling underscores its significant correlation with each stage of cancer pathogenesis and progression. The design and synthesis of MMP-9 inhibitors is a potentially attractive research area. Unfortunately, to date, there is no effective MMP-9 inhibitor that passes the clinical trials and is approved by the FDA. This review primarily focuses on exploring the diverse strategies employed in the design and advancement of MMP-9 inhibitors, along with their anticancer effects and selectivity. To illuminate the essential structural characteristics necessary for the future design of novel MMP-9 inhibitors, the current narrative review highlights several recently discovered MMP-9 inhibitors exhibiting notable selectivity and potency.
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spelling pubmed-104187712023-08-12 Novel Matrix Metalloproteinase-9 (MMP-9) Inhibitors in Cancer Treatment Rashid, Zainab Ahmed Bardaweel, Sanaa K. Int J Mol Sci Review Matrix metalloproteinases (MMPs) belong to a family of zinc-dependent proteolytic metalloenzymes. MMP-9, a member of the gelatinase B family, is characterized as one of the most intricate MMPs. The crucial involvement of MMP-9 in extracellular matrix (ECM) remodeling underscores its significant correlation with each stage of cancer pathogenesis and progression. The design and synthesis of MMP-9 inhibitors is a potentially attractive research area. Unfortunately, to date, there is no effective MMP-9 inhibitor that passes the clinical trials and is approved by the FDA. This review primarily focuses on exploring the diverse strategies employed in the design and advancement of MMP-9 inhibitors, along with their anticancer effects and selectivity. To illuminate the essential structural characteristics necessary for the future design of novel MMP-9 inhibitors, the current narrative review highlights several recently discovered MMP-9 inhibitors exhibiting notable selectivity and potency. MDPI 2023-07-28 /pmc/articles/PMC10418771/ /pubmed/37569509 http://dx.doi.org/10.3390/ijms241512133 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Rashid, Zainab Ahmed
Bardaweel, Sanaa K.
Novel Matrix Metalloproteinase-9 (MMP-9) Inhibitors in Cancer Treatment
title Novel Matrix Metalloproteinase-9 (MMP-9) Inhibitors in Cancer Treatment
title_full Novel Matrix Metalloproteinase-9 (MMP-9) Inhibitors in Cancer Treatment
title_fullStr Novel Matrix Metalloproteinase-9 (MMP-9) Inhibitors in Cancer Treatment
title_full_unstemmed Novel Matrix Metalloproteinase-9 (MMP-9) Inhibitors in Cancer Treatment
title_short Novel Matrix Metalloproteinase-9 (MMP-9) Inhibitors in Cancer Treatment
title_sort novel matrix metalloproteinase-9 (mmp-9) inhibitors in cancer treatment
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10418771/
https://www.ncbi.nlm.nih.gov/pubmed/37569509
http://dx.doi.org/10.3390/ijms241512133
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