Effects of VIP and VIPDAP on Proliferation and Lipid Peroxidation Metabolism in Human KB Cells
In the present study, we have utilized the transglutaminase (TGase) enzyme to modify the primary structure of VIP with diamminopropane (DAP) at the level of the Gln16. We have investigated the conformational stability of VIP and VIPDAP in solution by limited proteolysis experiments. The VIPDAP appears to be more resistant to the proteolytic attack of trypsin, thus indicating that the derivatization in position 16 is able to stabilize the structure of the peptide. However, we have studied their role in cell cycle modulation and antioxidant activity in the oropharyngeal epidermoid carcinoma KB cells
limited proteolysis cell cycle modulation vasoactive intestinal peptide vasoactive intestinal peptide analogs conformational analysis intracellular lipid peroxidation