Studies On Rational Design Of Affinity Ligands To Protein

Rational design of highly affinity ligands to proteins used by SYBYL on the basis of the structure of the proteins is presented, and successfully rational design the highly affinity ligand to Tissue Plasminogen Activator (t-PA).Firstly , the simulation was based on the results of the ELISA ofα-amylase ,lysozyme and insulin. Heptapeptides with high affinity specialty toα-amylase , lysozyme and insulin were docked into their proteins. Dscore, which was responding to the affinity, was found and proved effectively. Protein and Heptapeptides with high affinity specialty to it were docked and created a general MOLCAD surface. Electrostatic potential property (including hydrogen bond) and Van der Waals force play the important role in the affinity, but hydrophobic interaction is very weak. So we use Dscore to represent the affinity between ligand and protein.Amino acids location methods, FlexX and MOLCAD were used to rational design highly affinity peptide ligand (QDES) to t-PA. Electrostatic potential property (including hydrogen bond) and Van der Waals force play the important role in the affinity.Therefore structure-based design was proven to be an efficient route to develop a new affinity ligand for proteins.