Molecular Recognition of the Catalytic Zinc(II) Ion in MMP-13: Structure-Based Evolution of an Allosteric Inhibitor to Dual Binding Mode Inhibitors with Improved Lipophilic Ligand Efficiencies
Matrix metalloproteinases (MMPs) are a class of zinc dependent endopeptidases which play a crucial role in a multitude of severe diseases such as cancer and osteoarthritis. We employed MMP-13 as the target enzyme for the structure-based design and synthesis of inhibitors able to recognize the cataly...
Main Authors: | Thomas Fischer, Rainer Riedl |
---|---|
Format: | Article |
Language: | English |
Published: |
MDPI AG
2016-03-01
|
Series: | International Journal of Molecular Sciences |
Subjects: | |
Online Access: | http://www.mdpi.com/1422-0067/17/3/314 |
Similar Items
-
Development of a Non-Hydroxamate Dual Matrix Metalloproteinase (MMP)-7/-13 Inhibitor
by: Thomas Fischer, et al.
Published: (2017-09-01) -
Zinc Supported by Nitrogen-Rich Ligands: Applications Towards Catalytic Hydrosilylation And Modeling Zinc Enzymes
by: Ruccolo, Serge Michel
Published: (2016) -
Evaluation of zinc binding groups (ZBGs) as inhibitor building blocks using carbonic anhydrase and the catalytic domain of matrix metalloproteinase 12 (cdMMP-12)
by: Craig, Whitney Richert
Published: (2017) -
Nanoemulsion as a Platform for Iontophoretic Delivery of Lipophilic Drugs in Skin Tumors
by: Luciana Facco Dalmolin, et al.
Published: (2018-11-01) -
Investigation of Hydro-Lipophilic Properties of N-Alkoxyphenylhydroxynaphthalenecarboxamides †
by: Iva Kapustikova, et al.
Published: (2018-07-01)