Using optical tweezers to investigate the specific single-interaction between apoA-I molecule and ABCA1 on living cells

• 来源期刊: 中国光学快报（英文版）
• 年，卷（期）: 2013,（9）
• 页码范围: 76-79
• 页数: 4页
• 语种: 英文
• DOI: 10.3788/COL201311.091701

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±4.1pN.These results facilitate a pathological understanding of the mechanisms that underlie the specific interaction of apoA-I and ABCA1 at the single-molecule level.