Anantram, Aarti published the artcileMolecular dynamic simulations on an inhibitor of anti-apoptotic Bcl-2 proteins for insights into its interaction mechanism for anti-cancer activity, Quality Control of 518303-20-3, the publication is Journal of Biomolecular Structure and Dynamics (2019), 37(12), 3109-3121, database is CAplus and MEDLINE.
The first anticancer agents targeting this family of proteins were aimed primarily toward inhibition of Bcl-2. An elevated level of Mcl-1, despite Bcl-2 inhibition, continues to be a cause for resistance in most cancers. However, in silico exploration of Mcl-1 specific drugs and their associated mechanisms have not been clearly elucidated. In order to understand the same, we have carried out docking and mol. dynamic simulations on ABT-263 (Navitoclax), an orally active inhibitor of Bcl-2, Bcl-xL, and Bcl-w proteins; Obatoclax, a pan-Bcl-2 inhibitor as well as Maritoclax, an Mcl-1 specific inhibitor. Docking studies revealed that binding to the hydrophobic grooves is a prerequisite for action on the BCL protein and the binding mechanism and chem. space utilization dictates stability as well as specificity of the inhibitor mol. dynamic simulations showed that on binding, the a-helixes of these proteins exhibited less fluctuations than loop regions, also hydrophobic contacts and hydrogen bonding were observed to be the predominant interactions in the drug-receptor complexes.Communicated by Ramaswamy H. Sarma.
Journal of Biomolecular Structure and Dynamics published new progress about 518303-20-3. 518303-20-3 belongs to alcohols-buliding-blocks, auxiliary class Apoptosis,Bcl-2, name is 2-((4-(4-Bromophenylsulfonamido)-1-hydroxynaphthalen-2-yl)thio)acetic acid, and the molecular formula is C18H14BrNO5S2, Quality Control of 518303-20-3.
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