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. Author manuscript; available in PMC: 2015 Feb 1.
Published in final edited form as: Nat Mater. 2014 Jun 15;13(8):829–836. doi: 10.1038/nmat3998

Figure 1. Engineered fusion proteins with a β-sheet fibrillizing tail integrate into self-assembling peptide nanofibers.

Figure 1

a) Schematic representation of engineered fusion proteins having a β-sheet fibrillizing domain integrating into Q11 nanofibers. b-c) The βTail peptide underwent slow secondary structural transition from an α-helix to a β-sheet, whereas Q11 rapidly assembled into β-sheets, and a mutated βTail adopted a random coil structure (scale bar = 200 nm). A fusion of βTail and Green Fluorescent Protein-UV (βT GFP) efficiently integrated into Q11 nanofibers, whereas a fusion of Q11 and GFP (Q11-GFP) integrated moderately, and a fusion of GFP and a non-folding βTail mutant (βTmutant-GFP) integrated poorly, as demonstrated by (d) digital photographs of 1.5 mL microcentrifuge tubes, and (e) measured by fluorimetry of the supernatant above sedimented Q11 nanofiber solutions. f) βT-GFP also integrated into HK-Q11 and KFE8 nanofibers in a βTail-dependent manner, indicating that co-assembly was not limited to Q11-based nanofibers. N = 3, mean ± s.d. for e and f. * represents p < 0.05, ANOVA with Tukey's post-hoc. GFP adapted from PDB 1EMA in a.