TY - JOUR
T1 - Fibril growth behavior of amyloid β on polymer-based planar membranes
T2 - Implications for the entanglement and hydration of polymers
AU - Shimanouchi, Toshinori
AU - Iwamura, Miki
AU - Deguchi, Shintaro
AU - Kimura, Yukitaka
N1 - Funding Information:
Funding: This work was supported by Grant-in-Aid KAKEN (26249116) and the Okayama Foundation for Science and Technology (2014).
Publisher Copyright:
© 2021 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2021/5/2
Y1 - 2021/5/2
N2 - The design of biosensors and artificial organs using biocompatible materials with a low affinity for amyloid β peptide (Aβ) would contribute to the inhibition of fibril growth causing Alzheimer’s disease. We systematically studied the amyloidogenicity of Aβ on various planar mem-branes. The planar membranes were prepared using biocompatible polymers, viz., poly(methyl methacrylate) (PMMA), polysulfone (PSf), poly(L-lactic acid) (PLLA), and polyvinylpyrrolidone (PVP). Phospholipids from biomembranes, viz., 1,2-dioleoyl-phosphatidylcholine (DOPC), 1,2-dipalmitoyl-phosphatidylcholine (DPPC), and polyethylene glycol-graft-phosphatidyl ethanolamine (PEG-PE) were used as controls. Phospholipid-and polymer-based membranes were prepared to determine the kinetics of Aβ fibril formation. Rates of Aβ nucleation on the PSf-and DPPC-based membranes were significantly higher than those on the other membranes. Aβ accumulation, cal-culated by the change in frequency of a quartz crystal microbalance (QCM), followed the order: PSf > PLLA > DOPC > PMMA, PVP, DPPC, and PEG-PE. Nucleation rates exhibited a positive correlation with the corresponding accumulation (except for the DPPC-based membrane) and a negative correlation with the molecular weight of the polymers. Strong hydration along the polymer backbone and polymer–Aβ entanglement might contribute to the accumulation of Aβ and subsequent fibrillation.
AB - The design of biosensors and artificial organs using biocompatible materials with a low affinity for amyloid β peptide (Aβ) would contribute to the inhibition of fibril growth causing Alzheimer’s disease. We systematically studied the amyloidogenicity of Aβ on various planar mem-branes. The planar membranes were prepared using biocompatible polymers, viz., poly(methyl methacrylate) (PMMA), polysulfone (PSf), poly(L-lactic acid) (PLLA), and polyvinylpyrrolidone (PVP). Phospholipids from biomembranes, viz., 1,2-dioleoyl-phosphatidylcholine (DOPC), 1,2-dipalmitoyl-phosphatidylcholine (DPPC), and polyethylene glycol-graft-phosphatidyl ethanolamine (PEG-PE) were used as controls. Phospholipid-and polymer-based membranes were prepared to determine the kinetics of Aβ fibril formation. Rates of Aβ nucleation on the PSf-and DPPC-based membranes were significantly higher than those on the other membranes. Aβ accumulation, cal-culated by the change in frequency of a quartz crystal microbalance (QCM), followed the order: PSf > PLLA > DOPC > PMMA, PVP, DPPC, and PEG-PE. Nucleation rates exhibited a positive correlation with the corresponding accumulation (except for the DPPC-based membrane) and a negative correlation with the molecular weight of the polymers. Strong hydration along the polymer backbone and polymer–Aβ entanglement might contribute to the accumulation of Aβ and subsequent fibrillation.
KW - Amyloid fibril
KW - Amyloid β
KW - Biocompatible polymer
KW - Entanglement
KW - Hydration
KW - Hydration
KW - Nucleation
KW - Quartz crystal microbal-ance
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U2 - 10.3390/app11104408
DO - 10.3390/app11104408
M3 - Article
AN - SCOPUS:85106583867
VL - 11
JO - Applied Sciences (Switzerland)
JF - Applied Sciences (Switzerland)
SN - 2076-3417
IS - 10
M1 - 4408
ER -