title: Defining lipid-binding regions of human serum amyloid A using its fragment peptides.
abstract: Human serum amyloid A (SAA) protein is an apolipoprotein predominantly present in the high-density lipoprotein fraction of plasma. Despite its critical roles in lipid metabolism, especially in acute phases, systematic understanding of the lipid interaction of this protein is limited. Lipid-binding properties of synthetic fragment peptides corresponding to the N-terminal (residues 1-27), central (residues 43-63), and C-terminal (residues 77-104) parts of SAA molecule were examined. SAA (1-27) peptide binds to lipid forming an alpha-helical structure, whereas SAA (43-63) and (77-104) peptides do not display binding to lipid with any conformational changes. These results indicate that the N-terminal region of SAA is important for lipid interaction. In addition, the finding that deletion of or proline substitution in the most N-terminal region (residues 1-11) markedly decreased the binding to lipid further suggests that the alpha-helical structure in residues 1-11 is essential for lipid binding of SAA.
authors: Department of Biophysical Chemistry, Kobe Pharmaceutical University, 4-19-1 Motoyamakita-machi, Higashinada-ku, Kobe 658-8558, Japan.
authors: Shinya
authors: S
authors: Ohta
authors: Masafumi
authors: M
authors: Tanaka
authors: Kota
authors: K
authors: Sakakura
authors: Toru
authors: T
authors: Kawakami
authors: Saburo
authors: S
authors: Aimoto
authors: Hiroyuki
authors: H
authors: Saito
mesh_terms: D001665:Binding Sites; D002850:Chromatography, Gel; D002942:Circular Dichroism; D006801:Humans; D008055:Lipids / Q000737:chemistry*; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D000685:Serum Amyloid A Protein / Q000737:chemistry*; D013050:Spectrometry, Fluorescence
chemical_list: D008055:Lipids; D010446:Peptide Fragments; D000685:Serum Amyloid A Protein