In the present work, interactions between bovine serum albumin (BSA) with gemini surfactants were studied for their stabilization. A library of gemini surfactants has been designed on varying the cation and anion of parent surfactant. Geometry optimization of the surfactants has been performed by applying MOPAC approach to minimize energy of formation, where the RMS Gradient is set to 0.100. Further, molecular docking studies using iGEMDOCK software, was done to study the interaction between four hundred designed gemini surfactants molecyles and bouvine serum albumin (BSA). The binding between the BSA and surfactant was occurred due Vander Waals interaction, electrostatic interactions and hydrogen bonding, where the minimum binding energy approach were used to select the most potent compound. The molecular docking results successfully showed that, surfactant molecule are inserted into the cavity of BSA.
K. Vishvakarma, Vijay; Patel, Rajan; Kumari, Kamlesh; and Singh, Prashant
"Interaction between Bovine Serum Albumin and Gemini Surfactants Molecular Docking Characterization,"
Information Sciences Letters: Vol. 6
, Article 1.
Available at: https://digitalcommons.aaru.edu.jo/isl/vol6/iss2/1