TY - JOUR
T1 - ToF-SIMS observation for evaluating the interaction between amyloid β and lipid membranes
AU - Aoyagi, Satoka
AU - Shimanouchi, Toshinori
AU - Kawashima, Tomoko
AU - Iwai, Hideo
N1 - Funding Information:
The work was partly supported by NIMS microstructural characterization platform as a program of “Nanotechnology Platform” of the Ministry of Education, Culture, Sports, Science and Technology (MEXT), Japan. This work was also supported by a Grant-in-Aid for Scientific Research (No. 24686086) from the Ministry of Education, Science, Sports, and Culture of Japan (MEXT).
Publisher Copyright:
© 2015 Springer-Verlag Berlin Heidelberg.
PY - 2015/3/22
Y1 - 2015/3/22
N2 - Abstract The adsorption behaviour of amyloid beta (Aβ), thought to be a key peptide for understanding Alzheimer's disease, was investigated by means of time-of-flight secondary ion mass spectrometry (ToF-SIMS). Aβ aggregates depending on the lipid membrane condition though it has not been fully understood yet. In this study, Aβ samples on different lipid membranes, 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), were observed with ToF-SIMS and the complex ToF-SIMS data of the Aβ samples was interpreted using data analysis techniques such as principal component analysis (PCA), gentle-SIMS (G-SIMS) and g-ogram. DOPC and DMPC are liquid crystal at room temperature, while DPPC is gel at room temperature. As primary ion beams, Bi3+ and Ar cluster ion beams were used and the effect of an Ar cluster ion for evaluating biomolecules was also studied. The secondary ion images of the peptide fragment ions indicated by G-SIMS and g-ogram were consistent with the PCA results. It is suggested that Aβ is adsorbed homogeneously on the liquid-crystalline-phase lipid membranes, while it aggregates along the lipid on the gel-phase lipid membrane. Moreover, in the results using the Ar cluster, the influence of contamination was reduced.
AB - Abstract The adsorption behaviour of amyloid beta (Aβ), thought to be a key peptide for understanding Alzheimer's disease, was investigated by means of time-of-flight secondary ion mass spectrometry (ToF-SIMS). Aβ aggregates depending on the lipid membrane condition though it has not been fully understood yet. In this study, Aβ samples on different lipid membranes, 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC), 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and 1,2-dioleoyl-sn-glycero-3-phosphocholine (DOPC), were observed with ToF-SIMS and the complex ToF-SIMS data of the Aβ samples was interpreted using data analysis techniques such as principal component analysis (PCA), gentle-SIMS (G-SIMS) and g-ogram. DOPC and DMPC are liquid crystal at room temperature, while DPPC is gel at room temperature. As primary ion beams, Bi3+ and Ar cluster ion beams were used and the effect of an Ar cluster ion for evaluating biomolecules was also studied. The secondary ion images of the peptide fragment ions indicated by G-SIMS and g-ogram were consistent with the PCA results. It is suggested that Aβ is adsorbed homogeneously on the liquid-crystalline-phase lipid membranes, while it aggregates along the lipid on the gel-phase lipid membrane. Moreover, in the results using the Ar cluster, the influence of contamination was reduced.
KW - Amyloid beta
KW - Ar cluster beam
KW - Lipid
KW - Peptide structure
KW - ToF-SIMS
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U2 - 10.1007/s00216-015-8527-3
DO - 10.1007/s00216-015-8527-3
M3 - Article
C2 - 25687682
AN - SCOPUS:84938361728
SN - 0016-1152
VL - 407
SP - 2859
EP - 2863
JO - Fresenius Zeitschrift fur Analytische Chemie
JF - Fresenius Zeitschrift fur Analytische Chemie
IS - 10
M1 - 8527
ER -