The 4N1K peptide,which is derived from the C-terminal domain of thrombospondin-1(TSP-1),is usually used as a functional mimic peptide for TSP-1.Knowledge about the interaction force of 4N1K/CD47 is important in explai...The 4N1K peptide,which is derived from the C-terminal domain of thrombospondin-1(TSP-1),is usually used as a functional mimic peptide for TSP-1.Knowledge about the interaction force of 4N1K/CD47 is important in explaining how TSP-1 affects the biological effect of CD47.Here we used a single-molecule force spectroscopy(SMFS)technique to explore the interaction of 4N1K/CD47 on both normal and oxidative human red blood cells(h RBCs)at single-molecule level.There was no interaction force between 4N1K and CD47 on normal h RBCs;however,we did find 4N1K-bound CD47 on oxidative h RBCs.We also detected interaction forces for 4N1K/CD47ex(extracellular domain of human CD47),and 4N1K/oxidative CD47ex.The interaction forces of 4N1K/CD47ex were almost consistent with those of 4N1K/oxidative CD47ex at the same loading rate.These results suggest that the conformational change of CD47 is critical for 4N1K-CD47 interaction on oxidative h RBCs.展开更多
基金financially supported by the National Basic Research Program of China(2011CB933600,2013CB966900)the National Natural Science Foundation of China(21373200,81273334)Program for Changjiang Scholars and Innovative Research Team in University(PCSIRT,IRT1133)
文摘The 4N1K peptide,which is derived from the C-terminal domain of thrombospondin-1(TSP-1),is usually used as a functional mimic peptide for TSP-1.Knowledge about the interaction force of 4N1K/CD47 is important in explaining how TSP-1 affects the biological effect of CD47.Here we used a single-molecule force spectroscopy(SMFS)technique to explore the interaction of 4N1K/CD47 on both normal and oxidative human red blood cells(h RBCs)at single-molecule level.There was no interaction force between 4N1K and CD47 on normal h RBCs;however,we did find 4N1K-bound CD47 on oxidative h RBCs.We also detected interaction forces for 4N1K/CD47ex(extracellular domain of human CD47),and 4N1K/oxidative CD47ex.The interaction forces of 4N1K/CD47ex were almost consistent with those of 4N1K/oxidative CD47ex at the same loading rate.These results suggest that the conformational change of CD47 is critical for 4N1K-CD47 interaction on oxidative h RBCs.
