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Entrapment of Immature Amyloid Protofilaments in the Hydrophobic Domain of Schizophyllan

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Abstract

β-1,3-glucan schizophyllan (SPG) is known to adopt a triple helical structure in nature and a random coil conformation in alkaline solutions which forms a hydrophobic domain when its random coil is renatured. This paper presents the complexation of amyloid with SPG, presumably owing to hydrophobic interactions between the β-sheets and the SPG hydrophobic domain. Circular dichroism (CD) showed that complex had a negative band at 225 nm, indicating the presence of the stacked β-sheets. However, wide angle X-ray scattering (WAXS) showed no clear inter β-sheet diffractions that are generally observed at 1.0 nm in matured amyloid. Combining WAXS and CD, it can be concluded that lysozyme in complex has β-sheets but the β-sheets are not well stacked to give diffraction. Small angle X-ray scattering (SAXS) profile from complex can be reproduced using a combination of the cross-sectional Gunier and Debye-Bueche functions.

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Authors and Affiliations

  1. Department of Chemical Processes & Environments and Department of Chemistry, The University of Kitakyushu, 1-1 Hibikino, Wakamatu-ku, Kitakyushu, 808-0135, Fukuoka, Japan

    Mina Sakuragi, Yoichi Takeda, Naohiko Shimada & Kazuo Sakurai

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  1. Mina Sakuragi
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  2. Yoichi Takeda
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  3. Naohiko Shimada
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  4. Kazuo Sakurai
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Correspondence to Kazuo Sakurai.

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Sakuragi, M., Takeda, Y., Shimada, N. et al. Entrapment of Immature Amyloid Protofilaments in the Hydrophobic Domain of Schizophyllan . Polym. Bull. 61, 107–117 (2008). https://doi.org/10.1007/s00289-008-0927-5

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  • DOI: https://doi.org/10.1007/s00289-008-0927-5

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