Fig. 3: Biophysical analysis of PFNA–protein interactions.
From: Heat stable and intrinsically sterile liquid protein formulations
Representative transmission electron micrograph of monomeric BSA in saline (a) and amorphous protein aggregates (b) following unaided addition of the protein to PFOc. Scale bar in (a, b) represent 50 nm and 2 µm, respectively. c Representative transmission electron micrograph of PFNA-coated BSA assemblies in PFOc. Scale bar = 500 nm. d Magnified region of interest in (c) (white dashed box) showing individual PFNA-functionalized protein globules. Scale bar = 100 nm. Representative scanning electron micrographs of BSA in saline (e) or dispersed into PFOc via PFNA (f) before (25 °C) and after (100 °C) heating for 30 min. Scale bars = 50 µm. 1H (g) and 19F (h) NMR spectral regions of PFNA in PFOc before (maroon) and after (teal) coupling to BSA. Average wavenumber of BSA amide I (i) and amide II (j) bands before (−) and after (+) addition of PFNA. Average wavenumber of PFNA CF2 (i) and CF3 (j) bands before (−) and after (+) addition of BSA. Box plots shown in (i–l) represent data from n = 3 technical replicates, with line at mean and box bounds reflecting maxima and minima values. Statistical significance between conditions in panels i–l is indicated by a line using one-sided Student’s t-test. Source data for panels i–l are provided as a Source Data file.
