Abstract
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 (hRBCs) at single-molecule level. There was no interaction force between 4N1K and CD47 on normal hRBCs; however, we did find 4N1K-bound CD47 on oxidative hRBCs. 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 hRBCs.
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