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. 2021 Mar 4;16(3):e0248027. doi: 10.1371/journal.pone.0248027

Fig 3. Regulation of various Aβ peptide forms by human polymorphic SERPINA3.

Fig 3

(A) Representative TEM images of Aβ peptide at 72 hr preincubation. Typical fibrillar form was observed in Aβ 42 + SERPINA3 wild type; whereas Aβ 42 + SERPINA3 I308T still showed irregularly shaped oligomers as indicated by solid arrow and while open arrow indicated protofibrillar form. Scale bar: 100 nm. (B) Kinetics of amyloid β peptide oligomerization in presence of human SERPINA3. Here, x-axis shows prevalence of oligomer rich observation fields (in percentage) and y-axis shows preincubation time (hr). Significance levels were tested Aβ 42 + SERPINA3 I308T vs. Aβ 42 + SERPINA3 wild; Aβ 42 + SERPINA3 I308T vs. Aβ 42; Aβ 42 + SERPINA3 wild vs. Aβ 42. (n = 3, ** P ≤ 0.01. One-way ANOVA with Tukey and Kramer’s honestly significance difference test was used). (C) Thioflavin T fluorescence assay (data represent Mean ± SEM, n = 3). AFU refers arbitrary fluorescence units. (D) Representative images of thioflavin T fluorescence assay at 30 hrs. (E) Representative image of gradient gel native PAGE, showing Aβ 42 peptide in presence of human SERPINA3 recombinant proteins, at 0 to 48 hrs of preincubation. Open triangle showed presence of oligomeric Aβ peptide conformations. See also in S3 Fig.