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Imaging and measuring single-molecule interaction between a carbohydrate-binding module and natural plant cell wall cellulose.

Identifieur interne : 002A34 ( Main/Exploration ); précédent : 002A33; suivant : 002A35

Imaging and measuring single-molecule interaction between a carbohydrate-binding module and natural plant cell wall cellulose.

Auteurs : Mengmeng Zhang [États-Unis] ; Sheng-Cheng Wu ; Wen Zhou ; Bingqian Xu

Source :

RBID : pubmed:22849362

Descripteurs français

English descriptors

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.

DOI: 10.1021/jp304686q
PubMed: 22849362


Affiliations:


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Le document en format XML

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<div type="abstract" xml:lang="en">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.</div>
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