@article{oai:shiga-med.repo.nii.ac.jp:00003801,
 author = {柳沢, 大治郎 and 加藤, 智子 and 田口, 弘康 and 遠山, 育夫 and YANAGISAWA, Daijiro and KATO, Tomoko and TAGUCHI, Hiroyasu and SHIRAI, Nobuaki and HIRAO, Koichi and SOGABE, Takayuki and TOMIYAMA, Takami and GAMO, Keizo and HIRAHARA, Yukie and KITADA, Masaaki and TOOYAMA, Ikuo},
 journal = {Biomaterials},
 month = {Jan},
 note = {pdf, The accumulation of β-amyloid (Aβ) aggregates in the brain occurs early in the progression of Alzheimer's disease (AD), and non-fibrillar soluble Aβ oligomers are particularly neurotoxic. During binding to Aβ fibrils, curcumin, which can exist in an equilibrium state between its keto and enol tautomers, exists predominantly in the enol form, and binding activity of the keto form to Aβ fibrils is much weaker. Here we described the strong binding activity the keto form of curcumin derivative Shiga-Y51 shows for Aβ oligomers and its scant affinity for Aβ fibrils. Furthermore, with imaging mass spectrometry we revealed the blood-brain barrier permeability of Shiga-Y51 and its accumulation in the cerebral cortex and the hippocampus, where Aβ oligomers were mainly localized, in a mouse model of AD. The keto form of curcumin derivatives like Shiga-Y51 could be promising seed compounds to develop imaging probes and therapeutic agents targeting Aβ oligomers in the brain., Journal Article},
 title = {Keto form of curcumin derivatives strongly binds to Aβ oligomers but not fibrils.},
 volume = {270},
 year = {2021}
}