Imaging and Measuring Single-Molecule Interaction between a Carbohydrate-Binding Module and Natural Plant Cell Wall Cellulose
Citations Over TimeTop 10% of 2012 papers
Abstract
The affinitive interaction between a carbohydrate-binding module (CBM3a) and natural crystalline cellulose was visualized and measured at the single-molecule level. Noncontact high resolution imaging by atomic force microscopy (AFM) was used to follow the binding process, in real time, of CBM3a-functionalized 6 nm gold nanoparticles (GNPs) to the cell wall polymers on poplar stem sections. The GNP-CBM3a complexes were found to bind to the cellulose surface, closely aligning along the cellulose fibril axis. The binding details were further confirmed and studied by single-molecule recognition imaging and AFM single-molecule dynamic force spectroscopy (SMDFS) using a CBM3a-functionalized AFM tip. The unbinding force was measured to be 44.96 ± 18.80 pN under a loading rate of 67.2 nN/s. This research provides a radical method for the study of single-molecule affinity between CBM and cellulose that is critical to the engineering of novel cellulolytic enzymes.
Related Papers
- → Concurrent atomic force spectroscopy(2019)19 cited
- → AFM-Based Single-Molecule Force Spectroscopy of Proteins(2018)17 cited
- → Concurrent Atomic Force Spectroscopy(2018)1 cited
- Single Molecule Polymer Force Studies by AFM(2004)
- → Analysis of the force between DNA molecules and substrate in AFM-based manipulation process(2017)