Interactions of the Antitumor Macrolide Aplyronine A with Actin and Actin-Related Proteins Established by Its Versatile Photoaffinity Derivatives

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• 作者：Masaki Kita ; Yuichiro Hirayama ; Kota Yamagishi ; Kozo Yoneda ; Ryosuke Fujisawa ; Hideo Kigoshi
• 刊名：The Journal of the American Chemical Society
• 出版年：2012
• 出版时间：December 19, 2012
• 年：2012
• 卷：134
• 期：50
• 页码：20314-20317
• 全文大小：304K
• 年卷期：v.134,no.50(December 19, 2012)
• ISSN：1520-5126

文摘

The antitumor and apoptogenic macrolide aplyronine A (ApA) is a potent actin-depolymerizing agent. We developed an ApA acetylene analog that bears the aryldiazirine group at the C34 terminus, which formed a covalent bond with actin. With the use of the photoaffinity biotin derivatives of aplyronines A and C, Arp2 and Arp3 (actin-related proteins) were specifically purified as binding proteins along with actin from tumor cell lysate. However, Arp2 and Arp3 did not covalently bind to aplyronine photoaffinity derivatives. Thus, actin-related proteins might indirectly bind to ApA as the ternary adducts of the actin/ApA complex or through the oligomeric actin.