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Molecular docking analysis of curcumin analogues against kinase domain of ALK5.

ABSTRACT: During metastasis, cancer cells transcend from primary site to normal cells area upon attaining epithelial to mesenchymal transition (EMT) causing malignant cancer disease. Increased expression of TGF-? and its receptor ALK5 is an important hallmark of malignant cancer. In the present study, efficacy of curcumin and its analogues as inhibitors of ALK5 (TGF?R-I) receptor was evaluated using in silico approaches. A total of 142 curcumin analogues and curcumin were retrieved from peer reviewed literature and constructed a combinatorial library. Further their drug-likeness was assessed using Molinspiration, cheminformatics and preADMET online servers. The interaction of 142 curcumin analogues and curcumin with ALK5 receptor was studied using Autodock Vina. This study revealed six curcumin analogues as promising ALK5 inhibitors with significant binding energy and H-bonding interaction.

SUBMITTER: Kandagalla S

PROVIDER: S-EPMC5755696 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature

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Molecular docking analysis of curcumin analogues against kinase domain of ALK5.

Kandagalla Shivananda S Sharath B S BS Bharath Basavapattana Rudresh BR Hani Umme U Manjunatha Hanumanthappa H

In silico pharmacology 20171118 1

During metastasis, cancer cells transcend from primary site to normal cells area upon attaining epithelial to mesenchymal transition (EMT) causing malignant cancer disease. Increased expression of TGF-β and its receptor ALK5 is an important hallmark of malignant cancer. In the present study, efficacy of curcumin and its analogues as inhibitors of ALK5 (TGFβR-I) receptor was evaluated using in silico approaches. A total of 142 curcumin analogues and curcumin were retrieved from peer reviewed lite ...[more]

PMID: 29308351

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Correction to: Exploration for novel inhibitors showing back-to-front approach against VEGFR-2 kinase domain (4AG8) employing molecular docking mechanism and molecular dynamics simulations.

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