@misc{oai:kawasakigakuen.repo.nii.ac.jp:00000305,
 author = {Ryohei KONO and Sachiko NOMURA and Yoshiharu OKUNO and Tomoko UTSUNOMIYA and Hirotoshi UTSUNOMIYA},
 month = {Dec},
 note = {Protein misfolding is associated with formation of amyloid fibrils. Hen egg lysozyme, well-known for its structural properties, has been shown by atomic force microscopy to form needle-shaped amyloid fibrils under acidic conditions with high temperature. When disulfide bonds of hen lysozyme were reduced by reductant TCEP, it formed noodle-shaped amyloid fibrils. Difference in thioflavin T and 8-Anilino-1-naphthalenesulfonic acid (ANS) fluorescence of these fibrils suggested difference in structural properties. The needle-shaped amyloid fibrils exerted cytotoxicity on human neuroblastoma SH-SY5Y cells, but noodle-shaped amyloid fibrils did not. The reason for cytotoxicity being exerted only by needle-shaped amyloid fibrils was thought to be due to the difference in properties, such as fibril surface and inter-/intra-molecule structure. This finding indicates the importance of studying the interaction between the amyloid fibril surface and inter-/intra-molecular structural properties and cells. We also investigated whether Prunus mume extracts protect SH-SY5Y cells from hen lysozyme amyloid-induced toxicity. The Prunus mume seed extract protected the cells from needle-shaped amyloid toxicity. Prunus mume could therefore potentially prevent amyloid-related disease., Original Article},
 title = {Cytotoxicity of amyloid fibrils derived from hen lysozyme with different properties on SH-SY5Y and cytoprotective effect of prunus mume extracts},
 year = {2020}
}