期刊
BIOMOLECULES
卷 12, 期 4, 页码 -出版社
MDPI
DOI: 10.3390/biom12040594
关键词
adhesion maps; atomic force microscopy; jumping mode; molecular recognition imaging; rupture force; protein:ligand interactions; single molecule; protein detection
资金
- MCIN/AEI [PID2019-103901GB-I00]
- CSIC [QTP2103003]
- Government of Aragon-FEDER [E35_20R, LMP58_18]
Intermittent jumping force is an atomic force microscopy mode that provides simultaneous topography and maximum-adhesion images based on force spectroscopy. By scanning in a repulsive regime and applying very low forces, unspecific tip-sample forces can be avoided. This mode allows for qualitative and quantitative molecular recognition maps obtained at reasonably fast rates, which is advantageous for discriminating between similar protein molecules.
Intermittent jumping force is an operational atomic-force microscopy mode that produces simultaneous topography and tip-sample maximum-adhesion images based on force spectroscopy. In this work, the operation conditions have been implemented scanning in a repulsive regime and applying very low forces, thus avoiding unspecific tip-sample forces. Remarkably, adhesion images give only specific rupture events, becoming qualitative and quantitative molecular recognition maps obtained at reasonably fast rates, which is a great advantage compared to the force-volume modes. This procedure has been used to go further in discriminating between two similar protein molecules, avidin and streptavidin, in hybrid samples. The adhesion maps generated scanning with biotinylated probes showed features identified as avidin molecules, in the range of 40-80 pN; meanwhile, streptavidin molecules rendered 120-170 pN at the selected working conditions. The gathered results evidence that repulsive jumping force mode applying very small forces allows the identification of biomolecules through the specific rupture forces of the complexes and could serve to identify receptors on membranes or samples or be applied to design ultrasensitive detection technologies.
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