文章基本信息

标题：Oxidized Low-Density Lipoprotein-Binding Specificity of the Asp-Hemolysin-Related Synthetic Peptides from Aspergillus fumigatus
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作者：Takeshi Kumagai ; Hiromu Tsutsumi ; Norihiro Ogawa 等
期刊名称：Biological and Pharmaceutical Bulletin
印刷版ISSN：0918-6158
电子版ISSN：1347-5215
出版年度：2006
卷号：29
期号：11
页码：2181-2186
DOI：10.1248/bpb.29.2181
出版社：The Pharmaceutical Society of Japan
摘要：Oxidatively modified low-density lipoprotein (OxLDL) is present in atherosclerotic lesions and has been proposed to play an important role in atherogenesis. In the present study, in order to clarify the structure-binding activity relationship of Asp-hemolysin-related peptides to OxLDL, we investigated the interaction between Asp-hemolysin-related peptides consisting of 4 to 29 amino acid residues and OxLDL. The incubation of OxLDL with each Asp-hemolysin-related peptide resulted in the formation of an Asp-hemolysin/OxLDL complex. In particular, the tetrapeptide, YKDG (P-4), bound to OxLDL and inhibited the OxLDL-induced macrophage proliferation in a dose-dependent manner. Furthermore, we demonstrated that lysophosphatidylcholine (LysoPC) extracted from OxLDL inhibited the binding of P-21 to OxLDL in a dose-dependent manner and synthetic [¹⁴C]LysoPC bound to P-21. We propose here that the YKDG region is one of the important sites for the binding of these peptides to OxLDL, and LysoPC as a typical lipid moiety of OxLDL is attributed to the binding of OxLDL to these peptides.
关键词：Asp-hemolysin-related peptide;oxidized low-density lipoprotein;binding;lysophosphatidylcholine