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机构地区:[1]Key Laboratory for the Physics and Chemistry of Nanodevices,School of Electronics Engineering and Computer Science,Peking University [2]Department of Neurology,Peking University First Hospital
出 处:《Chinese Optics Letters》2013年第9期76-79,共4页中国光学快报(英文版)
基 金:supported by the National Basic Research Program of China(No.2011CB809100);the National Science and Technology Infrastructure Program of China(No.2012BAF14B14);the National Key Technologies R&D Program of China(No.2012ZX09303005003)
摘 要:We carry out in situ single-molecule measurements of the specific interaction between apolipoprotein A-I (apoA-I) and ATP binding cassette transporter A1 (ABCA1) on THP-1 cells. Single-molecule force spectroscopy shows that similar to normal apoA-I, the dysfunctional apoA-I from diabetes patients interacts with ABCA1 via two different binding sites on the cells. The strength of dysfunctional apoA-I binding to a high-capacity binding site is 26.5±4.9 pN. The minor direct apoA-I/ABCA1 binding strength is 56.7±4.1 pN. These results facilitate a pathological understanding of the mechanisms that underlie the specific interaction of aDoA-I and ABCA1 at the single-molecule level.We carry out in situ single-molecule measurements of the specific interaction between apolipoprotein A-I (apoA-I) and ATP binding cassette transporter A1 (ABCA1) on THP-1 cells. Single-molecule force spectroscopy shows that similar to normal apoA-I, the dysfunctional apoA-I from diabetes patients interacts with ABCA1 via two different binding sites on the cells. The strength of dysfunctional apoA-I binding to a high-capacity binding site is 26.5±4.9 pN. The minor direct apoA-I/ABCA1 binding strength is 56.7±4.1 pN. These results facilitate a pathological understanding of the mechanisms that underlie the specific interaction of aDoA-I and ABCA1 at the single-molecule level.
关 键 词:Binding sites Optical tweezers
分 类 号:R329[医药卫生—人体解剖和组织胚胎学]
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