Structural and bio-molecular interactions in human tenascin C and HIV: An in silico approach to avert AIDS, for infants under the exposure of HIV: Computational approach for avertion of AIDS in infants by breast milk

Eradication of HIV (Human Immuno-Deficiency Virus) via postnatal transmission, maintaining the nutritional benefits and immunologic advantages of the breast-feeding in infants is a primary outlook in today´s´ era. Documentation states that a HIV-arresting protein in the breast milk; human TNCs´ (tenascin-C) fibronectin domain obstructs the further interaction and signaling of responsible glycoprotein; gp120 from HIV for invading into the infants´ anatomy. So, essential savior human fibronectin III protein domain was homology modeled satisfactorily with the satisfaction of stereo-chemical parameters. Followed by its energy optimization, the human protein was docked with gp120 to study its detailed interaction pattern and binding modes. The optimized and simulated complex unveiled the polar charged residues, especially arginine from gp120 to exhibit a pivotal role. Conformational switches in gp120 before and after the indulgement of fibronectin III domain was computed, contrasted and analyzed. It was statistically significant with an overall coil-to-helix and coil-to-sheet transition. The statistically significant variation in the free energy of folding, viral protein folding rate, net area for solvent availability and electrostatic surface potential for gp120 also apprehended an efficient aversion from the membrane fusion and viral entry into the infants´ responsible cells, even though the mother remains HIV-carrier.