Design and synthesis of small chemical inhibitors containing different scaffolds for lck SH2 domain

Bioorg Med Chem Lett. 2003 Oct 20;13(20):3455-9. doi: 10.1016/s0960-894x(03)00735-2.


On the basis of the structure of (R)-rosmarinic acid, a series of small chemical compounds with a different scaffold was synthesized as inhibitors for lck SH2 domain. From ELISA results, most of all chemical compounds showed a similar or a little lower binding activity for lck SH2 domain compared to the lead compound, (R)-rosmarinic acid. It was characterized that the backbone rigidity between two catechol substructures was required for the full activity and acid substructure of the lead compound was important for the activity. We successfully identified novel lead compounds that did not contain phosphotyrosine moiety and might have an improved bioavailability as inhibitor for lck SH2 domain.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cinnamates / chemical synthesis*
  • Cinnamates / chemistry*
  • Depsides
  • Enzyme-Linked Immunosorbent Assay
  • Lymphocyte Specific Protein Tyrosine Kinase p56(lck) / chemistry*
  • Rosmarinic Acid
  • src Homology Domains


  • Cinnamates
  • Depsides
  • Lymphocyte Specific Protein Tyrosine Kinase p56(lck)