Fragment-based strategy for structural optimization in combination with 3D-QSAR

J Comput Aided Mol Des. 2013 Oct;27(10):897-915. doi: 10.1007/s10822-013-9687-x. Epub 2013 Nov 1.

Abstract

Fragment-based drug design has emerged as an important methodology for lead discovery and drug design. Different with other studies focused on fragment library design and active fragment identification, a fragment-based strategy was developed in combination with three-dimensional quantitative structure-activity relationship (3D-QSAR) for structural optimization in this study. Based on a validated scaffold or fragment hit, a series of structural optimization was conducted to convert it to lead compounds, including 3D-QSAR modelling, active site analysis, fragment-based structural optimization and evaluation of new molecules. 3D-QSAR models and active site analysis provided sufficient information for confirming the SAR and pharmacophoric features for fragments. This strategy was evaluated through the structural optimization on a c-Met inhibitor scaffold 5H-benzo[4,5]cyclohepta[1,2-b]pyridin-5-one, which resulted in an c-Met inhibitor with high inhibitory activity. Our study suggested the effectiveness of this fragment-based strategy and the druggability of our newly explored active region. The reliability of this strategy indicated it could also be applied to facilitate lead optimization of other targets.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Benzocycloheptenes / chemistry*
  • Catalytic Domain
  • Drug Design*
  • Humans
  • Models, Theoretical
  • Proto-Oncogene Proteins / antagonists & inhibitors*
  • Proto-Oncogene Proteins / chemistry
  • Pyridines / chemistry*
  • Quantitative Structure-Activity Relationship*
  • Receptor Protein-Tyrosine Kinases / antagonists & inhibitors*
  • Receptor Protein-Tyrosine Kinases / chemistry
  • Structure-Activity Relationship
  • c-Mer Tyrosine Kinase

Substances

  • 5H-benzo(4,5)cyclohepta(1,2-b)pyridin-5-one
  • Benzocycloheptenes
  • Proto-Oncogene Proteins
  • Pyridines
  • MERTK protein, human
  • Receptor Protein-Tyrosine Kinases
  • c-Mer Tyrosine Kinase