Journal:JBSD:26
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| - | <StructureSection load='' size='450' side='right' scene='' caption=''> | + | <StructureSection load='' size='450' side='right' scene='Journal:JBSD:26/Cv/7' caption=''> |
=== Investigation on the Site-Selective Binding of Bovine Serum Albumin by Erlotinib Hydrochloride === | === Investigation on the Site-Selective Binding of Bovine Serum Albumin by Erlotinib Hydrochloride === | ||
| - | <big>Yan Liu, Mingmao Chen, Zhipu Luo, Jingjing Lin, Ling Song</big> <ref> | + | <big>Yan Liu, Mingmao Chen, Zhipu Luo, Jingjing Lin, Ling Song</big> <ref>doi 10.1080/07391102.2012.726532</ref> |
<hr/> | <hr/> | ||
<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | The binding mode of erlotinib hydrochloride (ET), a targeted anticancer drug, to bovine serum albumin (BSA) was investigated through 1H NMR, spectroscopic, thermodynamic and molecular modeling methods. From these methods, the binding parameters, binding site, binding distance, and conformational changes were obtained. Site marker competitive experiments demonstrated that the binding site was located in the hydrophobic pocket of site I (subdomain IIA). The docking modeling agreed with the results of the fluorescence and displacement experiments. | + | The binding mode of <scene name='Journal:JBSD:26/Cv/2'>erlotinib hydrochloride (ET)</scene>, a targeted anticancer drug, to <scene name='Journal:JBSD:26/Cv/8'>bovine serum albumin (BSA)</scene> was investigated through 1H NMR, spectroscopic, thermodynamic and molecular modeling methods. Each subdomain is marked with a different colour (<font color='red'><b>red for subdomain IA</b></font>; <span style="color:orange;background-color:black;font-weight:bold;">orange, IB</span>; <span style="color:cyan;background-color:black;font-weight:bold;">cyan, IIA</span>; <span style="color:yellow;background-color:black;font-weight:bold;">yellow, IIB</span>; <span style="color:lime;background-color:black;font-weight:bold;">green, IIIA</span>; <font color='darkmagenta'><b>darkmagenta, IIIB</b></font>). From these methods, the binding parameters, binding site, binding distance, and conformational changes were obtained. Site marker competitive experiments demonstrated that the <scene name='Journal:JBSD:26/Cv/6'>binding site was located in the hydrophobic pocket of site I (subdomain IIA)</scene>. The docking modeling agreed with the results of the fluorescence and displacement experiments. |
</StructureSection> | </StructureSection> | ||
<references/> | <references/> | ||
__NOEDITSECTION__ | __NOEDITSECTION__ | ||
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- ↑ Liu Y, Chen M, Luo Z, Lin J, Song L. Investigation on the site-selective binding of bovine serum albumin by erlotinib hydrochloride. J Biomol Struct Dyn. 2012 Oct 17. PMID:23072300 doi:10.1080/07391102.2012.726532
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