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Virtual Screening: Using Molecular Docking and 3D‐QSAR Analysis of Matrix Metalloproteinase Inhibitors
Author(s) -
AmadorFalcón Laura,
RodríguezClavijo Daniela,
BaldirisÁvila Rosa,
ValdirisÁvila Verónica,
SalgadoMorán Guillermo,
GlossmanMitnik Daniel,
VivasReyes Ricardo
Publication year - 2013
Publication title -
journal of the chinese chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.329
H-Index - 45
eISSN - 2192-6549
pISSN - 0009-4536
DOI - 10.1002/jccs.201200459
Subject(s) - chemistry , matrix metalloproteinase , quantitative structure–activity relationship , docking (animal) , matrix metalloproteinase inhibitor , virtual screening , stereochemistry , glycoprotein , glycan , extracellular matrix , biochemistry , molecular model , combinatorial chemistry , computational biology , drug discovery , medicine , nursing , biology
Matrix metalloproteinase (MMPs) are a family of calcium‐dependent zinc‐containing endopeptidases which are responsible for the tissue remodeling and degradation of the extracellular matrix (ECM), including collagens, elastins, gelatin, matrix glycoproteins, and proteo‐ glycan. In this study, by using molecular docking and 3D‐QSAR analysis we get new insights into the relationship between experimental IC 50 values and their descriptors obtained from CoMSIA and CoMFA programs. Obtained information on molecular structural of a series of β‐N‐biaryl ether sulfonamide hydroxamates as potential MMP inhibitors, that can be used to understand the drug receptor interactions of these kind of molecules.