Effect of lipid environment on amyloid fibril formation of human serum amyloid A

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• 作者：Masafumi Tanaka^a ; ^{masatnk@kobepharma-u.ac.jp} ; Ayaka Nishimura^a ; Haruka Takeshita^a ; Hiroka Takase^a ; Toshiyuki Yamada^b ; Takahiro Mukai^a
• 关键词：CD ; circular dichroism ; CMC ; critical micelle concentration ; DLS ; dynamic light scattering ; HDL ; high-density lipoprotein ; PA ; phosphatidic acid ; PE ; phosphatidylethanolamine ; PC ; phosphatidylcholine ; PS ; phosphatidylserine ; SAA ; serum amyloid A ; Trp ; tryptophan ; ThT ; thioflavin T ; WMF ; wavelength of maximum fluorescence
• 刊名：Chemistry and Physics of Lipids
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：202
• 期：Complete
• 页码：6-12
• 全文大小：2448 K
• 卷排序：202

文摘

Amyloid fibril formation of human serum amyloid A (SAA) under a lipid environment was investigated. SAA (1–27) peptide bound to neutral and acidic, whereas SAA (43–63) peptide bound only to acidic lysophospholipids. For both these SAA peptides, binding to lysophospholipids inhibited heparin-induced amyloid-like fibril formation. Acidic lysophospholipids implied a possibility to promote fibril formation of SAA (1–27) peptide by themselves. Amyloid fibril formation of SAA may be modulated by altering the lipid head group composition of HDLs during metabolism.