Fig. 2: Comparative thermostability of chemically modified insulin analogs.
From: Synthesis of a highly thermostable insulin by phenylalanine conjugation at B29 Lysine
a Normalized ThT fluorescence intensity (λem) at 488 nm of HI and its derivatives (AcHI, PhacHI, AHI, and FHI). Data are represented as the mean of each group (N = 3) for each time point. Error bars represent the standard deviation; Circular Dichroism (CD) spectroscopy of (b) HI and (c) FHI, all CD experiments were carried out at 25 ± 0.1 °C using quartz cuvette with a path length of 1 mm; d Atomic Force Microscopy (AFM) micrographs of HI and FHI mounted over glass slide, incubated in 0.1 N HCl water (pH 1.6) containing 25 mM NaCl at 65 °C in different time intervals at concentration of 0.5 mg/mL (85 µM).
