Investigation of the binding modes between AIE-active molecules and dsDNA by single molecule force spectroscopy

Nanoscale ◽  
2015 ◽  
Vol 7 (19) ◽  
pp. 8939-8945 ◽  
Author(s):  
Ying Chen ◽  
Ke Ma ◽  
Ting Hu ◽  
Bo Jiang ◽  
Bin Xu ◽  
...  
Keyword(s):  
Single Molecule ◽  
Force Spectroscopy ◽  
Binding Modes ◽  
Single Molecule Force Spectroscopy ◽  
Aggregation Induced Emission ◽  
Double Stranded Dna

The binding modes between double-stranded DNA (dsDNA) and typical AIE (aggregation-induced emission)-active molecules were investigated using AFM-based single molecule force spectroscopy.

scholarly journals Single-Molecule Force Spectroscopy Reveals Multiple Binding Modes between DOPA and Different Rutile Surfaces

ChemPhysChem ◽  
2016 ◽  
Vol 18 (11) ◽  
pp. 1466-1469 ◽  
Author(s):  
Yiran Li ◽  
Huanyu Liu ◽  
Tiankuo Wang ◽  
Meng Qin ◽  
Yi Cao ◽  
...  
Keyword(s):  
Single Molecule ◽  
Force Spectroscopy ◽  
Binding Modes ◽  
Single Molecule Force Spectroscopy ◽  
Multiple Binding

scholarly journals Resolving dual binding conformations of cellulosome cohesin-dockerin complexes using single-molecule force spectroscopy

eLife ◽  
2015 ◽  
Vol 4 ◽  
Author(s):  
Markus A Jobst ◽  
Lukas F Milles ◽  
Constantin Schoeler ◽  
Wolfgang Ott ◽  
Daniel B Fried ◽  
...  
Keyword(s):  
Single Molecule ◽  
Molecular Conformation ◽  
Bacterial Species ◽  
Force Spectroscopy ◽  
Binding Mode ◽  
Site Directed Mutagenesis ◽  
Binding Modes ◽  
Single Molecule Force Spectroscopy ◽  
Vast Number ◽  
Knock Out

Receptor-ligand pairs are ordinarily thought to interact through a lock and key mechanism, where a unique molecular conformation is formed upon binding. Contrary to this paradigm, cellulosomal cohesin-dockerin (Coh-Doc) pairs are believed to interact through redundant dual binding modes consisting of two distinct conformations. Here, we combined site-directed mutagenesis and single-molecule force spectroscopy (SMFS) to study the unbinding of Coh:Doc complexes under force. We designed Doc mutations to knock out each binding mode, and compared their single-molecule unfolding patterns as they were dissociated from Coh using an atomic force microscope (AFM) cantilever. Although average bulk measurements were unable to resolve the differences in Doc binding modes due to the similarity of the interactions, with a single-molecule method we were able to discriminate the two modes based on distinct differences in their mechanical properties. We conclude that under native conditions wild-type Doc from Clostridium thermocellum exocellulase Cel48S populates both binding modes with similar probabilities. Given the vast number of Doc domains with predicteddual binding modes across multiple bacterial species, our approach opens up newpossibilities for understanding assembly and catalytic properties of a broadrange of multi-enzyme complexes.

Study on Intercalations between Double-Stranded DNA and Pyrene by Single-Molecule Force Spectroscopy: Toward the Detection of Mismatch in DNA

Langmuir ◽  
2010 ◽  
Vol 26 (17) ◽  
pp. 13773-13777 ◽  
Author(s):  
Zhenhua Jiang ◽  
Yiheng Zhang ◽  
Ying Yu ◽  
Zhiqiang Wang ◽  
Xi Zhang ◽  
...  
Keyword(s):  
Single Molecule ◽  
Force Spectroscopy ◽  
Single Molecule Force Spectroscopy ◽  
Double Stranded Dna
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