Single molecule force spectroscopy SMFS

Abstract Atomic force spectroscopy (AFM)-based single-molecule force spectroscopy (SMFS) was invented in the 1990s. Since then, SMFS has been developed into a powerful tool to study the inter- and intra-molecular interactions of macro-molecules. Using SMFS, a number of problems in the field of supramolecular chemistry and mechanochemistry have been studied at the single-molecule level, which are not accessible by traditional ensemble characterization methods. In this review, the principles of SMFS are introduced, followed by the discussion of several problems of contemporary interest at the interface of supramolecular chemistry and mechanochemistry of macromolecules, including single-chain elasticity of macromolecules, interactions between water and macromolecules, interactions between macromolecules and solid surface, and the interactions in supramolecular polymers. 

In another related approach, often referred to as single molecule force spectroscopy (SMFS), force measurements have also been used to determine the intramolecular forces within a range of biopolymeric molecules, including proteins, polysaccharides and nucleic acids. In such measurements, a molecule becomes attached to the probe surface during probe-sample contact (typically through physisorption) and then it is... 

The atomic force microscope (AFM) is not only a formidable instrument to image surfaces and immobilized supramolecular structures at very high spatial resolution but it is also a very interesting tool to quantitatively measure interaction forces. It is fair to conclude that AFM-based single-molecule force spectroscopy (SMFS) has matured in the past decade to become a reliable method to probe the rupture of individual supramolecular bonds and to analyze the strength of noncovalent interactions in a wide range... 

AFM-BASED SINGLE-MOLECULE FORCE SPECTROSCOPY (SMFS)... 

The capability of AFM to measure forces in the range of tens of picoNewtons has stimulated its application to study intermolecular and intramolecular forces stabilizing the fold of membrane proteins. The protein of interest is pulled out of the biological membrane by the AFM probe, and the force-distance spectrum depicts the force required to unfold the molecule in distinct steps as well as the contour length of the unfolded pol q)eptide. BR is one of the bestcharacterized membrane proteins by single-molecule force spectroscopy (SMFS). - When force spectroscopy measurements were applied to polytopic membrane proteins, the technique was shown to be sufficiently sensitive to detect forces between the transmembrane helices. - ... 

In order to improve selective antitumor therapy, dncent et al. successfully conjugated ceria nanoparticles to the tumor marker transferrin. They also combined single molecule force spectroscopy (SMFS)... 

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