Nanoparticle assisted magnetic resonance imaging of the early reversible stages of amyloid β self-assembly

2008 ◽  
pp. 2197 ◽  
Author(s):  
Jin-sil Choi ◽  
Hyuck Jae Choi ◽  
Dae Chul Jung ◽  
Joo-Hyuk Lee ◽  
Jinwoo Cheon
2010 ◽  
Vol 10 (1) ◽  
pp. 540-548 ◽  
Author(s):  
Kui Luo ◽  
Jing Tian ◽  
Gang Liu ◽  
Jiayu Sun ◽  
Chunchao Xia ◽  
...  

2019 ◽  
Vol 18 (12) ◽  
pp. 1376-1383 ◽  
Author(s):  
Yue Yuan ◽  
Jia Zhang ◽  
Xiaoliang Qi ◽  
Shuoguo Li ◽  
Guanshu Liu ◽  
...  

2020 ◽  
Vol 3 (11) ◽  
pp. 7752-7761
Author(s):  
Yilin He ◽  
Zheng Mao ◽  
Ye Zhang ◽  
Haiyin Lv ◽  
Jincong Yan ◽  
...  

Langmuir ◽  
2010 ◽  
Vol 26 (4) ◽  
pp. 2383-2391 ◽  
Author(s):  
Guozhen Liu ◽  
Charlotte E. Conn ◽  
Lynne J. Waddington ◽  
Stephen T. Mudie ◽  
Calum J. Drummond

Molecules ◽  
2021 ◽  
Vol 26 (5) ◽  
pp. 1362 ◽  
Author(s):  
Daijiro Yanagisawa ◽  
Nor Faeizah Ibrahim ◽  
Hiroyasu Taguchi ◽  
Shigehiro Morikawa ◽  
Takami Tomiyama ◽  
...  

Recent evidence suggests that the formation of soluble amyloid β (Aβ) aggregates with high toxicity, such as oligomers and protofibrils, is a key event that causes Alzheimer’s disease (AD). However, understanding the pathophysiological role of such soluble Aβ aggregates in the brain in vivo could be difficult due to the lack of a clinically available method to detect, visualize, and quantify soluble Aβ aggregates in the brain. We had synthesized a novel fluorinated curcumin derivative with a fixed keto form, named as Shiga-Y51, which exhibited high selectivity to Aβ oligomers in vitro. In this study, we investigated the in vivo detection of Aβ oligomers by fluorine-19 (19F) magnetic resonance imaging (MRI) using Shiga-Y51 in an APP/PS1 double transgenic mouse model of AD. Significantly high levels of 19F signals were detected in the upper forebrain region of APP/PS1 mice compared with wild-type mice. Moreover, the highest levels of Aβ oligomers were detected in the upper forebrain region of APP/PS1 mice in enzyme-linked immunosorbent assay. These findings suggested that 19F-MRI using Shiga-Y51 detected Aβ oligomers in the in vivo brain. Therefore, 19F-MRI using Shiga-Y51 with a 7 T MR scanner could be a powerful tool for imaging Aβ oligomers in the brain.


RSC Advances ◽  
2016 ◽  
Vol 6 (106) ◽  
pp. 104731-104734 ◽  
Author(s):  
Hecheng Zhang ◽  
Shan Peng ◽  
Suying Xu ◽  
Zhengguang Chen

A bifunctional protein nanospheres was successfully constructed through self-assembly of hydrolysed α-lactalbumin for magnetic resonance imaging and photodynamic therapy.


2019 ◽  
Vol 40 (9) ◽  
pp. 1849-1858 ◽  
Author(s):  
Per Kristian Eide ◽  
Lars Magnus Valnes ◽  
Are Hugo Pripp ◽  
Kent-Andre Mardal ◽  
Geir Ringstad

Impaired clearance of amyloid-β from choroid plexus is one proposed mechanism behind amyloid deposition in Alzheimer's disease. The present study examined whether clearance from choroid plexus of a cerebrospinal fluid tracer, serving as a surrogate marker of a metabolic waste product, is altered in idiopathic normal pressure hydrocephalus (iNPH), one sub-type of dementia. In a prospective observational study of close to healthy individuals (reference cohort; REF) and individuals with iNPH, we performed standardized T1-weighted magnetic resonance imaging scans before and through 24 h after intrathecal administration of a cerebrospinal fluid tracer (the magnetic resonance imaging contrast agent gadobutrol). Changes in normalized T1 signal within the choroid plexus and cerebrospinal fluid of lateral ventricles were quantified using FreeSurfer. The normalized T1 signal increased to maximum within choroid plexus and cerebrospinal fluid of lateral ventricles 6–9 h after intrathecal gadobutrol in both the REF and iNPH cohorts (enrichment phase). Peak difference in normalized T1 signals between REF and iNPH individuals occurred after 24 h (clearance phase). The results gave evidence for gadobutrol resorption from cerebrospinal fluid by choroid plexus, but with delay in iNPH patients. Whether choroid plexus has a role in iNPH pathogenesis in terms of delayed clearance of amyloid-β remains to be shown.


Stroke ◽  
2018 ◽  
Vol 49 (11) ◽  
pp. 2692-2698 ◽  
Author(s):  
Saima Hilal ◽  
M. Arfan Ikram ◽  
Marcel M. Verbeek ◽  
Oscar H. Franco ◽  
Erik Stoops ◽  
...  

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