TY - JOUR
T1 - Phosphatidylethanolamine accelerates aggregation of the amyloidogenic N-terminal fragment of apoA-I
AU - Kurimitsu, Naoko
AU - Mizuguchi, Chiharu
AU - Fujita, Kaho
AU - Taguchi, Suzuno
AU - Ohgita, Takashi
AU - Nishitsuji, Kazuchika
AU - Shimanouchi, Toshinori
AU - Saito, Hiroyuki
PY - 2020/5/1
Y1 - 2020/5/1
N2 - Membrane lipid composition is known to influence aggregation and fibril formation of many amyloidogenic proteins. Here, we found that phosphatidylethanolamine (PE) accelerates aggregation of the N-terminal 1‒83 fragment of an amyloidogenic G26R variant of apoA-I on lipid membranes. Circular dichroism and isothermal titration calorimetry measurements demonstrated that PE does not affect the α-helical structure and lipid binding property of apoA-I 1-83/G26R. Rather, fluorescence measurements indicated that PE induces more ordered lipid packing at the interfacial and acyl chain regions, providing more hydrophobic environments especially around the highly amyloidogenic regions in apoA-I on the membrane surface. These results suggest that PE promotes aggregation of the amyloidogenic N-terminal fragment of apoA-I on lipid membranes by inducing hydrophobic membrane environments.
AB - Membrane lipid composition is known to influence aggregation and fibril formation of many amyloidogenic proteins. Here, we found that phosphatidylethanolamine (PE) accelerates aggregation of the N-terminal 1‒83 fragment of an amyloidogenic G26R variant of apoA-I on lipid membranes. Circular dichroism and isothermal titration calorimetry measurements demonstrated that PE does not affect the α-helical structure and lipid binding property of apoA-I 1-83/G26R. Rather, fluorescence measurements indicated that PE induces more ordered lipid packing at the interfacial and acyl chain regions, providing more hydrophobic environments especially around the highly amyloidogenic regions in apoA-I on the membrane surface. These results suggest that PE promotes aggregation of the amyloidogenic N-terminal fragment of apoA-I on lipid membranes by inducing hydrophobic membrane environments.
KW - amyloid fibril
KW - apolipoprotein A-I
KW - lipid membrane
KW - phosphatidylethanolamine
KW - sphingomyelin
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U2 - 10.1002/1873-3468.13737
DO - 10.1002/1873-3468.13737
M3 - Article
C2 - 31968125
AN - SCOPUS:85078929306
VL - 594
SP - 1443
EP - 1452
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 9
ER -