Fig. 2: The glycoform and the stereochemistry of the glycosidic bond on Aβ9-21 influence its interaction with Aβ42. | Nature Communications

Fig. 2: The glycoform and the stereochemistry of the glycosidic bond on Aβ9-21 influence its interaction with Aβ42.

From: An O-glycopeptide participates in the formation of distinct Aβ42 fibril structures and attenuates Aβ42 neurotoxicity

Fig. 2

a Synthesis of glycosylated Aβ9-21. Reaction conditions: (i) microwave-assisted Fmoc-SPPS; (ii) 2, HATU, HOAt, DIEA, rt, 2 h×2; (iii) TFA/H2O/TIPS (95:2.5:2.5), rt, 2 h; (iv) 1 M NaOH, 1 h. (b) Circular dichroism (CD) spectra of Aβ42 and glycosylated Aβ9-21 (n = 3). The values are the means. c Thioflavin T (ThT) analysis of the aggregation processes of Aβ42 (6 μM) incubated with or without (glycosylated) Aβ9-21 (12 μM). d Plateau fluorescence calculated from the ThT kinetic curves in (c) (n = 3). e The binding affinity of (glycosylated) Aβ9-21 with Aβ42 measured by BLI. Statistical significance was assessed using one-way ANOVA test. All values are presented as the means ± s.e.m.s. Source data are provided as a Source Data file.

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