casein-kinase-ii and 3-8-dibromo-7-hydroxy-4-methylchromen-2-one

casein-kinase-ii has been researched along with 3-8-dibromo-7-hydroxy-4-methylchromen-2-one* in 2 studies

Other Studies

2 other study(ies) available for casein-kinase-ii and 3-8-dibromo-7-hydroxy-4-methylchromen-2-one

Article	Year
Docking and 3D-QSAR studies of 7-hydroxycoumarin derivatives as CK2 inhibitors. European journal of medicinal chemistry, 2010, Volume: 45, Issue:1 Protein kinase CK2 is involved in a broad range of physiological events. 3,8-dibromo-7-hydroxy-4-methylchromen-2-one (DBC) analogues show favorable inhibitory activity targeting CK2alpha. Two methods were used to build 3D-QSAR models for DBC derivatives. The ligand-based (LB) studies were performed based on the lower energy conformations employing atom fit alignment rule. The receptor-based (RB) models were also derived using bioactive conformations. Contour maps of RB CoMSIA model (q2=0.694, r2=0.916, N (no. of components)=7, r2(pred)=0.87) including the steric, electronic, hydrophobic and hydrogen bond acceptor fields were employed to explain factors affecting activities of inhibitors. The good consistency between the contour maps and the properties of CK2alpha amino acids provide useful hints for new inhibitors design. Topics: Casein Kinase II; Chromones; Drug Design; Emodin; Humans; Ligands; Models, Molecular; Protein Conformation; Protein Kinase Inhibitors; Quantitative Structure-Activity Relationship; Umbelliferones	2010
Coumarin as attractive casein kinase 2 (CK2) inhibitor scaffold: an integrate approach to elucidate the putative binding motif and explain structure-activity relationships. Journal of medicinal chemistry, 2008, Feb-28, Volume: 51, Issue:4 Casein kinase 2 (CK2) is an ubiquitous, essential, and highly pleiotropic protein kinase whose abnormally high constitutive activity is suspected to underlie its pathogenic potential in neoplasia and other diseases. Recently, using different virtual screening approaches, we have identified several novel CK2 inhibitors. In particular, we have discovered that coumarin moiety can be considered an attractive CK2 inhibitor scaffold. In the present work, we have synthetized and tested a small library of coumarins (more than 60), rationalizing the observed structure-activity relationship. Moreover, the most promising inhibitor, 3,8-dibromo-7-hydroxy-4-methylchromen-2-one (DBC), has been also crystallized in complex with CK2, and the experimental binding mode has been used to derive a linear interaction energy (LIE) model. Topics: Amino Acid Motifs; Binding Sites; Casein Kinase II; Chromones; Coumarins; Crystallography, X-Ray; Protein Binding; Structure-Activity Relationship; Thermodynamics; Zea mays	2008

Article

Year

Docking and 3D-QSAR studies of 7-hydroxycoumarin derivatives as CK2 inhibitors.

European journal of medicinal chemistry, 2010, Volume: 45, Issue:1

Protein kinase CK2 is involved in a broad range of physiological events. 3,8-dibromo-7-hydroxy-4-methylchromen-2-one (DBC) analogues show favorable inhibitory activity targeting CK2alpha. Two methods were used to build 3D-QSAR models for DBC derivatives. The ligand-based (LB) studies were performed based on the lower energy conformations employing atom fit alignment rule. The receptor-based (RB) models were also derived using bioactive conformations. Contour maps of RB CoMSIA model (q2=0.694, r2=0.916, N (no. of components)=7, r2(pred)=0.87) including the steric, electronic, hydrophobic and hydrogen bond acceptor fields were employed to explain factors affecting activities of inhibitors. The good consistency between the contour maps and the properties of CK2alpha amino acids provide useful hints for new inhibitors design.

Topics: Casein Kinase II; Chromones; Drug Design; Emodin; Humans; Ligands; Models, Molecular; Protein Conformation; Protein Kinase Inhibitors; Quantitative Structure-Activity Relationship; Umbelliferones

2010

Coumarin as attractive casein kinase 2 (CK2) inhibitor scaffold: an integrate approach to elucidate the putative binding motif and explain structure-activity relationships.

Journal of medicinal chemistry, 2008, Feb-28, Volume: 51, Issue:4

Casein kinase 2 (CK2) is an ubiquitous, essential, and highly pleiotropic protein kinase whose abnormally high constitutive activity is suspected to underlie its pathogenic potential in neoplasia and other diseases. Recently, using different virtual screening approaches, we have identified several novel CK2 inhibitors. In particular, we have discovered that coumarin moiety can be considered an attractive CK2 inhibitor scaffold. In the present work, we have synthetized and tested a small library of coumarins (more than 60), rationalizing the observed structure-activity relationship. Moreover, the most promising inhibitor, 3,8-dibromo-7-hydroxy-4-methylchromen-2-one (DBC), has been also crystallized in complex with CK2, and the experimental binding mode has been used to derive a linear interaction energy (LIE) model.

Topics: Amino Acid Motifs; Binding Sites; Casein Kinase II; Chromones; Coumarins; Crystallography, X-Ray; Protein Binding; Structure-Activity Relationship; Thermodynamics; Zea mays

2008