| 초록 |
Immobilization of proteins on biomaterial surfaces is important in various applications such as biosensors, biochips, and tissue engineering. However, non-covalently immobilized protein surfaces are not suitable for being repeated and long-term used, because non-covalently immobilized protein exists in equilibrium with solution and can therefore be gradually lost during the use. This problem can be overcome by covalent conjugation, which offers long-lasting immobilization. Transferrin, the iron transport glycoprotein in mammals, is known to involve in iron metabolism and normal cell growth. Many diseases (cancer, anemia, malaria, tuberculosis) are related with transferrin concentration in serum. In the present investigation, we have prepared covalently immobilized apo and holo transferrin on self-assembled monolayer. Various techniques such as X-ray, atomic force microscopy and x-ray photo electron spectroscopy have been used to characterize the immobilized protein surfaces. |
