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. Author manuscript; available in PMC: 2014 Feb 7.
Published in final edited form as: Nanoscale. 2012 Dec 21;5(3):1105–1115. doi: 10.1039/c2nr33215a

Fig. 8. Cell aggregation, Als1 unfolding and cell surface hydrophobicity require amyloid interactions.

Fig. 8

(a, b, c) Micrograph (a), optical microscopy (b) and overlaid optical and fluorescence microscopy (c) images of C. albicans WT cells grown in the presence of 50 ng ml−1 caspofungin and 100 μM thioflavin T (ThT) documenting the inhibition of cell aggregation by ThT. (d, g) Adhesion force maps (1 μm × 1 μm, color scale: 350 pN) recorded in buffer with an adhesion peptide-tip (d) or a hydrophobic-tip (g) on C. albicans WT cells grown in the presence of caspofungin (50 ng ml−1), harvested and further treated with 100 μM ThT. (e, h) Corresponding adhesion force histograms (n = 1024) together with representative force curves. (f, i) Histograms of rupture distances (n = 1024), and 3-D reconstructed polymer maps (false colors, adhesion forces in green for peptide-tip and orange for hydrophobic-tip).