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Altuntas, T.G. et al.

Altuntas, Olgen, Nebioglu, Akaho,

A study on the interaction between p60 c-Src receptor tyrosine kinase and arylcarboxylic and arylacetic acid derivatives based on docking modes and in vitro activity.

The fundamental role that receptor tyrosine kinases play in cancer and other proliferative diseases has provided the impetus for an extensive effort on the part of both academic and pharmaceutical laboratories to develop highly specific inhibitors. In this study, inhibitory activity of previously synthesized arylacetic and arylcarboxylic acid derivatives were examined against substrate of tyrosine kinase. It can be assumed that the activity of compounds becomes higher when the -CH(2) linkage exist between aromatic ring and the amide group of the side chain. In addition, when the R(1) and R(2) substitutents are methyl group in both series, the higher activity observed. The data obtained from docking study (DOCK4.0) indicated that compounds 2, 4, 7, 8, 11 render satisfactory interaction with the active site of enzyme, Lys295 of p60(c-Src) tyrosine kinase. Comparison of this interaction and the evaluation of biological data showed that compound 4 is the most active among the entire derivatives.[1]

References

A study on the interaction between p60 c-Src receptor tyrosine kinase and arylcarboxylic and arylacetic acid derivatives based on docking modes and in vitro activity. Altuntas, T.G., Olgen, S., Nebioglu, D., Akaho, E. Biol. Pharm. Bull. (2004) [Pubmed]

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