Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2006-5-4
pubmed:abstractText
The binding features of a series of 5-lipoxygenase (5-LOX) inhibitors (caffeic acid, NDGA, AA-861, CDC, esculetin, gossypol and phenidone) to human 5-LOX have been studied by using surface plasmon resonance biosensor (SPR) technology based Biacore 3000 and molecular docking simulation analyses. The SPR results showed that the equilibrium dissociation constant (KD) values evaluated by Biacore 3000 for the inhibitors showed a good correlation with its reported IC50, suggesting that SPR technology might be applicable as a direct assay method in screening new 5-LOX inhibitors at an early stage. In addition, the 3D structural model of 5-LOX was generated according to the crystal structure of rabbit reticulocyte 15-lipoxygenase, and the molecular docking simulation analyses revealed that the predicted binding free energies for the inhibitors correlated well with the KD values measured by SPR assay, which implies the correctness of the constructed 3D structural model of 5-LOX. This current work has potential for application in structure-based 5-LOX inhibitor discovery.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
139
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
715-23
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:16672272-Amino Acid Sequence, pubmed-meshheading:16672272-Animals, pubmed-meshheading:16672272-Arachidonate 5-Lipoxygenase, pubmed-meshheading:16672272-Arachidonic Acid, pubmed-meshheading:16672272-Binding, Competitive, pubmed-meshheading:16672272-Cells, Cultured, pubmed-meshheading:16672272-Computer Simulation, pubmed-meshheading:16672272-Enzyme Inhibitors, pubmed-meshheading:16672272-Enzymes, Immobilized, pubmed-meshheading:16672272-Humans, pubmed-meshheading:16672272-Kinetics, pubmed-meshheading:16672272-Lipoxygenase Inhibitors, pubmed-meshheading:16672272-Models, Molecular, pubmed-meshheading:16672272-Molecular Sequence Data, pubmed-meshheading:16672272-Protein Binding, pubmed-meshheading:16672272-Protein Conformation, pubmed-meshheading:16672272-Protein Structure, Tertiary, pubmed-meshheading:16672272-Quantitative Structure-Activity Relationship, pubmed-meshheading:16672272-Sequence Homology, Amino Acid, pubmed-meshheading:16672272-Surface Plasmon Resonance
pubmed:year
2006
pubmed:articleTitle
Binding investigation of human 5-lipoxygenase with its inhibitors by SPR technology correlating with molecular docking simulation.
pubmed:affiliation
Drug Discovery and Design Center, State Key Laboratory of Drug Research, Shanghai Institute of Materia Medica, Shanghai Institutes for Biological Sciences, Graduate School of the Chinese Academy of Sciences, Shanghai, China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't