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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...
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