kh-1060 and Neoplasms

kh-1060 has been researched along with Neoplasms* in 1 studies

Other Studies

1 other study(ies) available for kh-1060 and Neoplasms

Article	Year
Assessment of the free binding energy of 1,25-dihydroxyvitamin D3 and its analogs with the human VDR receptor model. Acta biochimica Polonica, 2012, Volume: 59, Issue:4 1,25-dihydroxyvitamin D(3) has quite significant anticancer properties, but its strong calcemic effect in principle excludes it as a potential anticancer drug. Currently, a lot of effort is being devoted to develop potent anticancer analogs of 1,25-dihydroxyvitamin D(3) that would not induce hypercalcemia during therapy. In this work, the free binding energy of the VDR receptor with 1,25-dihydroxyvitamin D(3) and its three potent analogs (EB 1089, KH 1060 and RO 25-9022) is calculated and compared with each other. With this approach, we could estimate the relative binding affinity of the most potent analog, RO 25-9022, and also revealed a quite distinct mechanism of its interaction with VDR. Topics: Antineoplastic Agents; Binding Sites; Calcitriol; Cell Line, Tumor; Crystallography, X-Ray; Energy Metabolism; Humans; Hypercalcemia; Ligands; Molecular Docking Simulation; Neoplasms; Protein Binding; Protein Conformation; Receptors, Calcitriol	2012

Article

Year

Assessment of the free binding energy of 1,25-dihydroxyvitamin D3 and its analogs with the human VDR receptor model.

Acta biochimica Polonica, 2012, Volume: 59, Issue:4

1,25-dihydroxyvitamin D(3) has quite significant anticancer properties, but its strong calcemic effect in principle excludes it as a potential anticancer drug. Currently, a lot of effort is being devoted to develop potent anticancer analogs of 1,25-dihydroxyvitamin D(3) that would not induce hypercalcemia during therapy. In this work, the free binding energy of the VDR receptor with 1,25-dihydroxyvitamin D(3) and its three potent analogs (EB 1089, KH 1060 and RO 25-9022) is calculated and compared with each other. With this approach, we could estimate the relative binding affinity of the most potent analog, RO 25-9022, and also revealed a quite distinct mechanism of its interaction with VDR.

Topics: Antineoplastic Agents; Binding Sites; Calcitriol; Cell Line, Tumor; Crystallography, X-Ray; Energy Metabolism; Humans; Hypercalcemia; Ligands; Molecular Docking Simulation; Neoplasms; Protein Binding; Protein Conformation; Receptors, Calcitriol

2012