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A Computational Study to Prevent HIV Invasion by Bovine LF in Mucosal- Layer via Blocking of DC-SIGN_GP120 Interaction

Author(s):

Arundhati Banerjee, Rakhi Dasgupta and Sujay Ray*   Pages 1 - 12 ( 12 )

Abstract:


Background: Invasion of HIV in human occurs through DC-SIGN’s interaction via the mucosal lining during sexual transmission. Bovine lactoferrin (bLF) has been known to hinder this invasion via its interaction with DC-SIGN. Hitherto, protein assays have been undergone but molecular-level studies remained unexplored.

Methodology: The 3D structures of the three proteins were studied. After protein docking (bLF_DC-SIGN and gp120_DC-SIGN), the complexes underwent simulation. Stability parameters and binding patterns with residues were explored.

Results and Conclusion: ΔG values, net area for solvent accessibilities and conformational fluctuations in DC-SIGN affirms the binding of bLF with DC-SIGN to be more spontaneous and steadier contrary to that with gp120. Residue participation inferred more interactions to occur from bLF complex with greater percentage of arginine (which strengthens the interaction) while electrostatic interaction between Lys45 (bLF) and Glu26 (DC-SIGN) strengthened the complex. Arg37 played an active role from DC-SIGN to form the stabilizing charged-neutral H-bond, while Lys63 from bLF formed two more such stabilizing charged-neutral H-bond with DC-SIGN. The prime binding sites in DC-SIGN; Arg37 and Gln34 occupy helices. The binding pockets in DC-SIGN may be blocked by bLF spontaneously, to hinder their interaction with gp120. No ionic-ionic interaction was observed from gp120_DC-SIGN complex. 88th residue which was a predominant residue in the binding pocket was found to experience a conformational shift from coils to sheets after interaction of DC-SIGN with bLF. This would instigate the pharmaceutical research as non-toxic LF would be economic as a remarkable peptide inhibitor opposing HIV.

Keywords:

Bovine Lactoferrin, Dendritic Cells, HIV Peptide Inhibitor, Sexual Transmission, Protein Interacting Residues, Simulation succeeding Minimization

Affiliation:

Department of Biochemistry and Biophysics, University of Kalyani, Kalyani, Nadia, Department of Biochemistry and Biophysics, University of Kalyani, Kalyani, Nadia, Amity Institute of Biotechnology, Amity University, Kolkata



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