MULTISCALE COMPUTATION ANALYSIS OF INTERACTION BETWEEN MANNOSE AND LIGHT SUBUNIT MUSHROOM TYROSINASE (LSMT) USING MOLECULAR DOCKING AND ONIOM (OUR OWN N-LAYERED INTEGRATED MOLECULAR ORBITALS AND MOLECULAR MECHANICS)

• Main Author: Aswin
• Format: Theses
• Language: Indonesia
• Online Access: https://digilib.itb.ac.id/gdl/view/39921
• Institution: Institut Teknologi Bandung

A novel protein like-lectin Light subunit Mushroom Tyrosinase (LSMT) was discovered during elucidation of the button mushroom Agaricus bisporus tyrosinse structure. LSMT share high structural homology with Ricin-B like lectin from mushroom Clotucybe botulinum nebularis (CNL) and HA-33 from Clostridium botulinum. Both of the protein were known to recognize sugar group on intestine surface and possess ability to inhibit the breeding of breast cancer cell. The benefit of the protein lead to promising usage of LSMT to develop as a drug carrier and also supported its ability not evoke the immune reaction in the body. This study was focused on preliminary investigation between mannose and LSMT using molecular docking and ONIOM (our Own N-layered Integrated molecular Orbitals and molecular Mechanics). Molecular docking calculation revealed three possible binding positions, of which the first resembles the sugar-binding region in the structures of its homolog (HA-33 or CNL) and the second is located in the interface region to the tyrosinase subunit. Another position is a new finding region that includes interaction with five amino acid residues at least. Calculation result in full DFT by traction model of complex each amino acid residue and mannose demonstrated the interaction in C2 of pyranose ring of mannose was occurred in Glu86. However, the interaction energy of the complex resulted the highest of energy and the interaction took place in the backbone of Glu86. ONIOM calculation involved entire of protein complex system recovered the calculation, in which the lowest energy and interaction in side chain of Glu86 obtained.