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|Title:||Discovery of novel ligands using phage display||Authors:||Nur Azri Muhamad Azan||Keywords:||DRNTU::Engineering||Issue Date:||2016||Abstract:||Cellular interactions with their surroundings are pivotal for cells to function. These interactions are facilitated by a number of receptors found on the surface of cells, bound to specific glycoproteins found in the extracellular matrix (ECM). For epithelial cells, laminin-5 has been proven to be a crucial component of the basement membrane. Primarily, it serves to anchor cells to the basal lamina and is involved in multiple processes such as tissue remodelling and wound healing. However, it also influences cell behaviour via interactions with integral membrane proteins (integrin). Receptors are extremely selective and sensitive to their binding molecule, as with α3β1 and α6β4, and laminin-5. Due to the limited research conducted on α6β4, which is involved in processes like the invasion of cancer cells and formation of hemidesmosomes, this study aims to establish the relationship for the interaction between α6β4 and laminin-5. Recombinant laminin-globular 3 (rLG3) from laminin-5 was developed and purified in order to be used to study the binding affinity with α3β1 and α6β4 via ELISA test. However, the test showed there was insignificant optical density against the concentration of α6β4. This indicates that the binding of α6β4 does not occur at the LG3 domain of laminin-5. A different approach towards determining the binding site for α6β4 on laminin-5 should be utilised to understand the interaction between integrin and receptor. This knowledge has significant impact on cell behaviour and cellular processes, and can influence future applications in multiple fields such as regenerative medicine and tissue engineering.||URI:||http://hdl.handle.net/10356/66392||Rights:||Nanyang Technological University||Fulltext Permission:||restricted||Fulltext Availability:||With Fulltext|
|Appears in Collections:||MSE Student Reports (FYP/IA/PA/PI)|
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