Literature DB >> 20139908

Structural studies of B-type Aurora kinase inhibitors using computational methods.

Mm Neaz1, M Muddassar, Fa Pasha, Seung Joo Cho.   

Abstract

AIM: To characterize the structural features of quinazoline-based Aurora B inhibitors that influence its inhibitor activity.
METHODS: Two geometrical methods, Method 1 and Method 2, were used to develop the 3D-QSAR models. The most active ligand was used as the template for the alignment of all the ligands in Method 1, and a conformer of the cocrystal ligand was used as the template for the alignment of all the ligands in Method 2.
RESULTS: The models suggest that highly active ligands can be designed by varying the R1 substituent at position 7 of the quinazoline ring with positively charged, bulky, hydrophobic groups, while bulky and hydrophobic groups around the thiazole ring are desirable for higher activity.
CONCLUSION: This study emphasizes that the bioactive conformer is rather different from the minima. The steric, electrostatic, and hydrophobic field effects contribute to its inhibitory activity.

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Year:  2010        PMID: 20139908      PMCID: PMC4002836          DOI: 10.1038/aps.2009.188

Source DB:  PubMed          Journal:  Acta Pharmacol Sin        ISSN: 1671-4083            Impact factor:   6.150


  44 in total

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Authors:  R Giet; D M Glover
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  1 in total

1.  3D-QSAR and molecular docking studies on derivatives of MK-0457, GSK1070916 and SNS-314 as inhibitors against Aurora B kinase.

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  1 in total

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