Amyloid-β<sub>42</sub> (Aβ<sub>42</sub>) accumulates within senileplaque, a pathological hall mark of Alzheimer’s disease (AD). Our previous reports showed that the monoclonal antibodies 37-...Amyloid-β<sub>42</sub> (Aβ<sub>42</sub>) accumulates within senileplaque, a pathological hall mark of Alzheimer’s disease (AD). Our previous reports showed that the monoclonal antibodies 37-11 and 77-3 react with conformational epitopes on the surface of the soluble aggregates of Aβ<sub>42</sub> and that sandwich ELISA using these two monoclonal antibodies yields high reactivity to detect soluble aggregates of Aβ<sub>42</sub>. Here, the reactivity of the sandwich ELISA was shown to increase in the presence of 50 μM Cu<sup>2+</sup>. However, the addition of Cu<sup>2+</sup> had only a small effect on the reactivity of a direct ELISA using antibody 37-11 or 77-3, suggesting that Cu<sup>2+</sup> has a small effect on the number of epitopes on the surface of the aggregates. Atomic force microscopy images showed that larger aggregates were formed in the presence of Cu<sup>2+</sup>, as shown in the other reports. Cu<sup>2+</sup> may gather the aggregates with distinct epitopes recognized by antibodies 37-11 and 77-3, leading to increased signal intensity of the sandwich ELISA.展开更多
The accumulation of solubleβ-amyloid aggregates(sAβs)is one of the main culprits in Alzheimer’s disease(AD)progression,which can lead to synaptic dysfunction and subsequent neurodegeneration.Herein,we describe a na...The accumulation of solubleβ-amyloid aggregates(sAβs)is one of the main culprits in Alzheimer’s disease(AD)progression,which can lead to synaptic dysfunction and subsequent neurodegeneration.Herein,we describe a nanoscavenger with novel structure that can cross the blood–brain barrier(BBB),accurately collect neurotoxic sAβs,and facilitate amounts ofβ-amyloid(Aβ)clearance.展开更多
文摘Amyloid-β<sub>42</sub> (Aβ<sub>42</sub>) accumulates within senileplaque, a pathological hall mark of Alzheimer’s disease (AD). Our previous reports showed that the monoclonal antibodies 37-11 and 77-3 react with conformational epitopes on the surface of the soluble aggregates of Aβ<sub>42</sub> and that sandwich ELISA using these two monoclonal antibodies yields high reactivity to detect soluble aggregates of Aβ<sub>42</sub>. Here, the reactivity of the sandwich ELISA was shown to increase in the presence of 50 μM Cu<sup>2+</sup>. However, the addition of Cu<sup>2+</sup> had only a small effect on the reactivity of a direct ELISA using antibody 37-11 or 77-3, suggesting that Cu<sup>2+</sup> has a small effect on the number of epitopes on the surface of the aggregates. Atomic force microscopy images showed that larger aggregates were formed in the presence of Cu<sup>2+</sup>, as shown in the other reports. Cu<sup>2+</sup> may gather the aggregates with distinct epitopes recognized by antibodies 37-11 and 77-3, leading to increased signal intensity of the sandwich ELISA.
基金supported by the National Key Research and Development Programs of China(grant no.2018YFA0209700)the National Natural Science Foundation of China(NSFC+4 种基金grant nos.51673100 and 21620102005)the Fundamental Research Funds for the Central Universities(Nankai Universitygrant nos.ZB19100123 and ZB16008705)the Tianjin Natural Science Foundation(grant no.18JCQNJC03600)the China Postdoctoral Science Foundation(grant no.2019M660975).
文摘The accumulation of solubleβ-amyloid aggregates(sAβs)is one of the main culprits in Alzheimer’s disease(AD)progression,which can lead to synaptic dysfunction and subsequent neurodegeneration.Herein,we describe a nanoscavenger with novel structure that can cross the blood–brain barrier(BBB),accurately collect neurotoxic sAβs,and facilitate amounts ofβ-amyloid(Aβ)clearance.
