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Trivalent metal ions based on inorganic compounds with in vitro inhibitory activity of matrix metalloproteinase 13

Paper ID Volume ID Publish Year Pages File Format Full-Text
16754 42610 2016 9 PDF Available
Title
Trivalent metal ions based on inorganic compounds with in vitro inhibitory activity of matrix metalloproteinase 13
Abstract

•Refolding the recombinant histidine-tagged cdMMP-13 using size exclusion chromatography (SEC).•The catalytic domain of collagenase-3 is a 23 kDa protein.•Analysis the inhibitory activity of metal ions to cdMMP-13 in vitro.•K3[Fe(CN)6] exhibit cdMMP-13 inhibitory potential with a half maximal inhibitory concentration (IC50) of 1.3 μM.•Develop the medicinal value of K3[Fe(CN)6] for future drug screening.

Collagenase-3 (MMP-13) inhibitors have attracted considerable attention in recent years and have been developed as a therapeutic target for a variety of diseases, including cancer. Matrix metalloproteinases (MMPs) can be inhibited by a multitude of compounds, including hydroxamic acids. Studies have shown that materials and compounds containing trivalent metal ions, particularly potassium hexacyanoferrate (III) (K3[Fe(CN)6]), exhibit cdMMP-13 inhibitory potential with a half maximal inhibitory concentration (IC50) of 1.3 μM. The target protein was obtained by refolding the recombinant histidine-tagged cdMMP-13 using size exclusion chromatography (SEC). The secondary structures of the refolded cdMMP-13 with or without metal ions were further analyzed via circular dichroism and the results indicate that upon binding with metal ions, an altered structure with increased domain stability was obtained. Furthermore, isothermal titration calorimetry (ITC) experiments demonstrated that K3[Fe(CN)6]is able to bind to MMP-13 and endothelial cell tube formation tests provide further evidence for this interaction to exhibit anti-angiogenesis potential. To the best of our knowledge, no previous report of an inorganic compound featuring a MMP-13 inhibitory activity has ever been reported in the literature. Our results demonstrate that K3[Fe(CN)6] is useful as a new effective and specific inhibitor for cdMMP-13 which may be of great potential for future drug screening applications.

Keywords
Collagenase-3 catalytic domain; Metal ions; Protein refolding; Circular dichroism spectral; Isothermal titration calorimetry; Endothelial tube formation
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Trivalent metal ions based on inorganic compounds with in vitro inhibitory activity of matrix metalloproteinase 13
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 92, October 2016, Pages 9–17
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us