Video imaging by high speed atomic force microscopy of collagenase movement on collagen fibrils

2014 Fiscal Year Final Research Report

• Project/Area Number: 25870262
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Biophysics; Chemical biology
• Research Institution: Kanazawa University
• Principal Investigator: NAKAYAMA Takahiro 金沢大学, バイオAFM先端研究センター, 助教 (00532821)
• Project Period (FY): 2013-04-01 – 2015-03-31
• Keywords: 酵素反応の化学力学共役 / １分子観察 / 原子間力顕微鏡 / コラーゲン / コラゲナーゼ

Outline of Final Research Achievements

To reveal the mechanism by which collagenases degrade collagen fibrils, we observed and analyzed the collagenase movement on the collagen quaternary structure. High-speed atomic force microscopy, which allows simultaneous observation of the enzyme movement and the substrate structure, is effective for achieving the goal of this study. We observed and analyzed the collagenase behavior Our results clearly visualized that bacterial collagenases bind on and degrade from the lateral edge of collagen fibrils and that hierarchical structure of collagen prevents collagenase molecules from engaging in collagenolytic reactions. In addition, we also demonstrated that the bacterial collagenase molecules move on collagen fibrils from the amino- to the carboxyl terminus of collagen molecules, depending on their activities.

Free Research Field

生物物理学