%0 Journal Article
%T MEMBRANE INSERTION OF Aβ WOULD INDUCE ITS FIBRIL FORMATION<br>淀粉样蛋白Aβ的插膜作用可以抑制其形成纤维
%A JI Shang-rong
%A WU Yi
%A SUI Sen-fang
%A <br>吉尚戎
%A 武一
%A 隋森芳
%J 生物物理学报
%D 2004
%I 
%X a-Amyloid peptide (A a ), the core protein of amyloid plaques in Alzheimer's disease, is a mixture of multilength peptides which are all derived from the amyloid precursor protei n (APP), and A a 40 and A a 42 are the two major components of the mixture. The effects of me mbrane cholesterol and buffer pH on the fibril formation of A a 40 and A a 42 were investigated respectively in this paper. The observation of electronic microscopy showed that cholesterol-containing liposome could nearl y completely inhibit the fibril formation of A a 40, and low pH could partly inhibit the fibrils formation of A a 42. Monolayer approach showed that A a 40 and A a 42 both were inclined to insert into membrane under the two above conditions. Further conformational measurements showed that the membrane in sertion had different effects on the secondary structure of A a 40 and A a 42. Therefore, the results of this paper indicate that the mechanisms to inh ibit the fibril formation of the two proteins are different, while the membrane insertion of A a 40 or A a 42 can reduce the fibril formation to a certain extent.
%K a-Amyloid peptide
%K Fibril formation
%K Liposome
%K EM observation
%K Membrane inser tion
%K CD spectra<br>纤维形成
%K 脂质体
%K 电镜观察
%K 插膜
%K 圆二色光谱
%K β-淀粉样蛋白
%K 老年性痴呆症
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=E0C9D9BBED813D6674AC13E942EAC86D&aid=16B7AEA53C0BF0A5&yid=D0E58B75BFD8E51C&vid=A04140E723CB732E&iid=CA4FD0336C81A37A&sid=DF92D298D3FF1E6E&eid=59906B3B2830C2C5&journal_id=1000-6737&journal_name=生物物理学报&referenced_num=1&reference_num=19