Abstract
Amyloid beta (Aβ) adsorption onto lipid membranes depending on the condition of a lipid was investigated by means of time-of-flight secondary ion mass spectrometry (ToF-SIMS). Aβ aggregation depending on the different hardness of lipid membrane has not been clarified yet although it is important to understand Alzheimer's disease. Aβ (1-40) on three different lipid membranes having different transition temperatures has been evaluated using ToF-SIMS in the previous study, and in this study, the differences between Aβ on liquid crystalline-phase lipid membranes and that on gel-phase lipid membranes were investigated in order to clarify the mechanisms of aggregation and peptide folding change. ToF-SIMS secondary ion images clearly showed Aβ distribution on lipid membranes. Because ToF-SIMS data is extremely complicated although it contains rich information, it was analysed by principal component analysis (PCA). Score images indicated by PCA are consistent with the images of secondary ions related to Aβ and are clearer than the secondary ion images. Moreover, PCA results suggest the difference between Aβ on different lipid membranes in terms of amino acid fragment ions, and the orientation of Aβ on 1,2-dipalmitoyl-sn-glycero-3-phosphocholine was indicated.
| Original language | English |
|---|---|
| Journal | Surface and Interface Analysis |
| DOIs | |
| Publication status | Accepted/In press - 2016 |
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Keywords
- Amyloid beta
- Lipid
- Structural analysis
- ToF-SIMS
ASJC Scopus subject areas
- Chemistry(all)
- Condensed Matter Physics
- Surfaces and Interfaces
- Materials Chemistry
- Surfaces, Coatings and Films
Cite this
The structural evaluation of amyloid beta on lipid membranes. / Aoyagi, Satoka; Iwamura, Miki; Shimanouchi, Toshinori; Yokoyama, Yuta; Iwai, Hideo.
In: Surface and Interface Analysis, 2016.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The structural evaluation of amyloid beta on lipid membranes
AU - Aoyagi, Satoka
AU - Iwamura, Miki
AU - Shimanouchi, Toshinori
AU - Yokoyama, Yuta
AU - Iwai, Hideo
PY - 2016
Y1 - 2016
N2 - Amyloid beta (Aβ) adsorption onto lipid membranes depending on the condition of a lipid was investigated by means of time-of-flight secondary ion mass spectrometry (ToF-SIMS). Aβ aggregation depending on the different hardness of lipid membrane has not been clarified yet although it is important to understand Alzheimer's disease. Aβ (1-40) on three different lipid membranes having different transition temperatures has been evaluated using ToF-SIMS in the previous study, and in this study, the differences between Aβ on liquid crystalline-phase lipid membranes and that on gel-phase lipid membranes were investigated in order to clarify the mechanisms of aggregation and peptide folding change. ToF-SIMS secondary ion images clearly showed Aβ distribution on lipid membranes. Because ToF-SIMS data is extremely complicated although it contains rich information, it was analysed by principal component analysis (PCA). Score images indicated by PCA are consistent with the images of secondary ions related to Aβ and are clearer than the secondary ion images. Moreover, PCA results suggest the difference between Aβ on different lipid membranes in terms of amino acid fragment ions, and the orientation of Aβ on 1,2-dipalmitoyl-sn-glycero-3-phosphocholine was indicated.
AB - Amyloid beta (Aβ) adsorption onto lipid membranes depending on the condition of a lipid was investigated by means of time-of-flight secondary ion mass spectrometry (ToF-SIMS). Aβ aggregation depending on the different hardness of lipid membrane has not been clarified yet although it is important to understand Alzheimer's disease. Aβ (1-40) on three different lipid membranes having different transition temperatures has been evaluated using ToF-SIMS in the previous study, and in this study, the differences between Aβ on liquid crystalline-phase lipid membranes and that on gel-phase lipid membranes were investigated in order to clarify the mechanisms of aggregation and peptide folding change. ToF-SIMS secondary ion images clearly showed Aβ distribution on lipid membranes. Because ToF-SIMS data is extremely complicated although it contains rich information, it was analysed by principal component analysis (PCA). Score images indicated by PCA are consistent with the images of secondary ions related to Aβ and are clearer than the secondary ion images. Moreover, PCA results suggest the difference between Aβ on different lipid membranes in terms of amino acid fragment ions, and the orientation of Aβ on 1,2-dipalmitoyl-sn-glycero-3-phosphocholine was indicated.
KW - Amyloid beta
KW - Lipid
KW - Structural analysis
KW - ToF-SIMS
UR - http://www.scopus.com/inward/record.url?scp=84979777186&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84979777186&partnerID=8YFLogxK
U2 - 10.1002/sia.6086
DO - 10.1002/sia.6086
M3 - Article
AN - SCOPUS:84979777186
JO - Surface and Interface Analysis
JF - Surface and Interface Analysis
SN - 0142-2421
ER -