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Keywords: catch bonds; differential scanning calorimetry; fluorescence; irreversible denaturation; parallel plate flow chamber; pause time; peptide binding circular dichroism; thermodynamics; von Willebrand factor.To understand the effect of the N-terminal peptide on the function of the A1-domain of vWF, the protein was expressed with (A1-1238) and without the N-terminal peptide (A1-1261). We used a flow chamber to measure the dynamics of platelet interactions with A1-1238 and A1-1261. Each domain variant was immobilized on glass slides with a modified chelating chemistry that enabled surface capture via the N-terminally fused histidine tag. This method ensured reproducible capture of the proteins eliminating possible structural issues associated with nonspecific immobilization on plastic or glass. The slides were completely inert to platelets. of citrated whole blood followed by Tris-buffered saline was perfused at low shear to enable platelets to attach to the surface immobilized domains. After red cells were perfused away with buffer, the translocation of the remaining attached platelets over the surfaces was recorded at each shear rate and the velocities and pause times calculated from the coordinate data of each platelet on the surface as described in the methods. hows the pause time data as a function of shear rate along with the number of platelet tracks analyzed from each movie. A1-1261 has longer pause times than A1-1238 indicating that the presence of the covalently linked N-terminal sequence decreases the time for which platelets remain attached. In addition, the translocation velocities were increased for A1-1238 relative to A1-1261. To determine if this N-terminal sequence could inhibit the catch bond when free in solution, we incubated surface immobilized A1-1261 with excess free peptide and added the free peptide to of whole blood and to our perfusion buffer and performed the assay. The result was a significant decrease in pause times to the levels of that obtained for A1-1238 and an increase in translocation velocities. Addition of free N-terminal peptide to A1-1238 or a peptide with the same amino acid composition, but a scrambled sequence, to either A1-1238 or A1-1261 did not significantly change the pause times or translocation velocities observed in the absence of peptide.

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Author: A1Domains A1Domains

A1Domains A1Domains

Member since: Jul 01, 2021
Published articles: 7

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