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  • Title: Binding modes of cibacron blue with albumin in affinity chromatography using docking tools.
    Author: Kılıç S, Andaç M, Denizli A.
    Journal: Int J Biol Macromol; 2021 Jul 31; 183():110-118. PubMed ID: 33915211.
    Abstract:
    Affinity chromatography is a standard method, which used for protein purification and separation studies due to its specificity and selectivity. There are several affinity chromatography methods, such as dye affinity, immobilized metal chelated affinity, and affinity electrophoresis. Cibacron Blue F3G-A (CBD), as a dye ligand, is one of the most used dyes among dye affinity chromatography. CBD is ideally suited for human serum albumin (HSA) separation and purification in affinity chromatography for several years. However, even though CBD has many purification applications, there is not much research focused on the interaction between CBD and HSA in molecular docking. The interactions between CBD and HSA were simulated via AutoDock molecular docking software in this study. Investigated possibilities resulted in six different conformations on different locations, which light the way to variable connectivity of CBD. Thus, it was determined that the most favorable binding is conformation 5, with its lowest binding energy, which is energetically favorable.
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