Fig. 3: Properties of GY23 variant coacervates (5 mg/mL) formed at pH = 8.0 buffers with 1 M ionic strength fixed by NaCl. | Communications Chemistry

Fig. 3: Properties of GY23 variant coacervates (5 mg/mL) formed at pH = 8.0 buffers with 1 M ionic strength fixed by NaCl.

From: Tuning the viscoelastic properties of peptide coacervates by single amino acid mutations and salt kosmotropicity

Fig. 3

a Storage modulus (G’) and loss modulus (G”) of peptide coacervates. b Complex viscosity (η) of peptide coacervates. c G’, G” and η of coacervates formed by GY23 variants with A→F mutations at the sweep frequency of 0.1 Hz. Data are presented as the mean ± SD of n = 3 independent experiments. d SFA force-distance curves of GY23 peptide variant coacervates. All peptides formed coacervates at the test conditions, expect for GY23-7A/F-10A/F and 7 A/F-10A/F-18A/F, which formed precipitates due to stronger peptide-peptide interactions. e FRAP images and relative fluorescence intensities of GY23 (top) and GY23-9F/L coacervate microdroplets (bottom). Data presented as mean ± SD. t0.5 indicates the time required to achieve 50% recovery of maximum intensity. t0.5 of GY23-9F/L is significantly lower than GY23, two-sided Student’s t test, *P < 0.05.

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