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.