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. 2015 Dec 10;7(3):1738–1752. doi: 10.1039/c5sc04194e

Fig. 3. TEM analysis of HD6 self-assembly and SEM analysis of bacterial agglutination. Top row: transmission electron micrographs of 10 mM sodium phosphate pH 7.4 (control), 0.4 μM trypsin (control), 20 μM proHD6 in the absence and presence of 0.4 μM trypsin, and 20 μM HD6. All the samples were incubated at room temperature for 1 h. Scale bar = 100 nm. TEM images obtained using 10 mM Tris-maleate pH 6.4 are presented in Fig. S7. Middle row: scanning electron micrographs of E. coli ATCC 25922 treated with 50 mM Tris-maleate pH 6.4 (control), 0.4 μM APMSF-inactivated trypsin (control), 3 μM proHD6, 3 μM trypsin-cleaved proHD6, or 3 μM HD6. Trypsin-cleaved proHD6 was prepared prior to incubation with the bacteria and the residual enzymatic activity was inhibited by APMSF (Experimental section). Following a 30 min incubation, the bacterial suspensions were centrifuged, fixed, and analyzed by SEM. Scale bar = 20 μm. Bottom row: SEM of L. monocytogenes ATCC19115 treated under the same conditions as in the middle row. Scale bar = 20 μm. Additional SEM images are shown in Fig. S9–S12. .

Fig. 3