Fig. 3: Heme causes a major reduction in the antiparallel β sheet component of fibril-forming aggregates. | Communications Biology

Fig. 3: Heme causes a major reduction in the antiparallel β sheet component of fibril-forming aggregates.

From: Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects

Fig. 3

Deconvoluted FT-IR spectra of 24 h oligomers incubated a in the absence of heme; or b in presence of heme from the beginning of incubation period (oligomers1, preincubation); c depicts the IR spectrum of oligomers2 formed when 48 h prefibrillar and fibrillar aggregates were treated with heme, postincubation. d Addition of heme causes a drastic reduction in the antiparallel β sheet component (bands at ~1680–90 cm−1, Panels ac, illustrated in red) of the resulting oligomeric population. The bands depicted in green denote the parallel β sheet component (1622–1638 cm−1). Error bars are ±SEM obtained from four independent experiments. Second derivatives of the FT-IR spectra (Supplementary Fig. 5, SI) have been used to determine individual peaks.

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