|
|
|
|
| LEADER |
01000naa a22002652 4500 |
| 001 |
NLM293092265 |
| 003 |
DE-627 |
| 005 |
20231225074544.0 |
| 007 |
cr uuu---uuuuu |
| 008 |
231225s2019 xx |||||o 00| ||eng c |
| 024 |
7 |
|
|a 10.1021/acs.langmuir.8b03599
|2 doi
|
| 028 |
5 |
2 |
|a pubmed24n0976.xml
|
| 035 |
|
|
|a (DE-627)NLM293092265
|
| 035 |
|
|
|a (NLM)30681866
|
| 040 |
|
|
|a DE-627
|b ger
|c DE-627
|e rakwb
|
| 041 |
|
|
|a eng
|
| 100 |
1 |
|
|a Hao, Xiuping
|e verfasserin
|4 aut
|
| 245 |
1 |
0 |
|a Seeding and Cross-Seeding Aggregations of Aβ40 and Its N-Terminal-Truncated Peptide Aβ11-40
|
| 264 |
|
1 |
|c 2019
|
| 336 |
|
|
|a Text
|b txt
|2 rdacontent
|
| 337 |
|
|
|a ƒaComputermedien
|b c
|2 rdamedia
|
| 338 |
|
|
|a ƒa Online-Ressource
|b cr
|2 rdacarrier
|
| 500 |
|
|
|a Date Completed 22.06.2020
|
| 500 |
|
|
|a Date Revised 22.06.2020
|
| 500 |
|
|
|a published: Print-Electronic
|
| 500 |
|
|
|a Citation Status MEDLINE
|
| 520 |
|
|
|a In the amyloid plaques of Alzheimer's disease (AD) patients, a large number of N-terminal-truncated amyloid β (Aβ) peptides such as Aβ11-40 have been identified in addition to the full-length Aβ peptides. However, little is known about the roles of the N-terminal-truncated peptides in AD pathological process. Herein, seeding and cross-seeding aggregations of Aβ40 and its N-terminal-truncated Aβ11-40 were investigated in the solution and on the surfaces of chips with immobilized seeds by extensive biophysical and biological analyses. The results showed that Aβ40 and Aβ11-40 aggregates could seed both homologous and heterologous aggregations of the two monomers. However, the capability and characteristics of the seeding (homologous aggregation) and cross-seeding (heterologous aggregation) were significantly different. Aβ40 seeds showed stronger acceleration effects on the aggregations than Aβ11-40 seeds and induced β-sheet-rich fibrous aggregates of similar cytotoxicities for the two monomers. This indicates that Aβ40 and Aβ11-40 had similar aggregation pathways in the seeding and cross-seeding on Aβ40 seeds. By contrast, Aβ11-40 seeds led to different aggregation pathways of Aβ40 and Aβ11-40. Pure Aβ11-40 aggregates had higher toxicity than Aβ40 aggregates, and as seeds, Aβ11-40 seeds induced Aβ40 to form aggregates of higher cytotoxicity. However, homologous Aβ11-40 aggregates induced by Aβ11-40 seeds showed lower cytotoxicity than pure Aβ11-40 aggregates. The results suggest that Aβ11-40 plays an important role in the pathological process of AD
|
| 650 |
|
4 |
|a Journal Article
|
| 650 |
|
4 |
|a Research Support, Non-U.S. Gov't
|
| 650 |
|
7 |
|a Amyloid beta-Peptides
|2 NLM
|
| 650 |
|
7 |
|a Immobilized Proteins
|2 NLM
|
| 650 |
|
7 |
|a Peptide Fragments
|2 NLM
|
| 650 |
|
7 |
|a amyloid beta-protein (1-40)
|2 NLM
|
| 650 |
|
7 |
|a amyloid beta-protein (11-40)
|2 NLM
|
| 700 |
1 |
|
|a Zheng, Jie
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Sun, Yan
|e verfasserin
|4 aut
|
| 700 |
1 |
|
|a Dong, Xiaoyan
|e verfasserin
|4 aut
|
| 773 |
0 |
8 |
|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1992
|g 35(2019), 7 vom: 19. Feb., Seite 2821-2831
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
|
| 773 |
1 |
8 |
|g volume:35
|g year:2019
|g number:7
|g day:19
|g month:02
|g pages:2821-2831
|
| 856 |
4 |
0 |
|u http://dx.doi.org/10.1021/acs.langmuir.8b03599
|3 Volltext
|
| 912 |
|
|
|a GBV_USEFLAG_A
|
| 912 |
|
|
|a SYSFLAG_A
|
| 912 |
|
|
|a GBV_NLM
|
| 912 |
|
|
|a GBV_ILN_22
|
| 912 |
|
|
|a GBV_ILN_350
|
| 912 |
|
|
|a GBV_ILN_721
|
| 951 |
|
|
|a AR
|
| 952 |
|
|
|d 35
|j 2019
|e 7
|b 19
|c 02
|h 2821-2831
|