|Publication type:||Article in scientific journal|
|Type of review:||Peer review (publication)|
|Title:||Design and structural evolution of matrix metalloproteinase inhibitors|
|Published in:||Chemistry – A European Journal|
|Publisher / Ed. Institution:||Wiley|
|Subjects:||Drug desgin; Drug discovery; Inhibitors; Medicinal chemistry; Metalloenzyme; Animal; Human; Matrix metalloproteinase inhibitors; Matrix metalloproteinases; Molecular model; Structure-activity relationship|
|Subject (DDC):||615: Pharmacology and therapeutics|
|Abstract:||Matrix metalloproteinases (MMPs) are involved in a multitude of severe diseases. Despite MMPs being considered druggable targets, past drug-discovery programs have not delivered the anticipated clinical benefits. This review examines the latest structural evolution of small-molecule inhibitors of MMPs, with a focus on the development of novel chemical entities with improved affinity and selectivity profiles. X-ray crystallographic data of the protein targets and cocrystal structures with inhibitors proved to be key for the success achieved during this ambitious endeavor. An evolutionary view on the structural diversity generated for this class of molecules is provided. This encouraging development paves the way for the clinical utilization of this class of highly relevant therapeutic targets. The structure-based design of superior MMP inhibitors highlights the power of this technique and displays strategies for the development of treatment options based on the modulation of challenging drug targets.|
|Fulltext version:||Published version|
|License (according to publishing contract):||Licence according to publishing contract|
|Departement:||Life Sciences and Facility Management|
|Organisational Unit:||Institute of Chemistry and Biotechnology (ICBT)|
|Appears in collections:||Publikationen Life Sciences und Facility Management|
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