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Article

Molecular Recognition of Proteins through Quantitative Force Maps at Single Molecule Level

by 1,2,*,†, 1,† and 1,2,3,*,†
1
Instituto de Nanociencia y Materiales de Aragón (INMA), CSIC-Universidad de Zaragoza, 50018 Zaragoza, Spain
2
Laboratorio de Microscopias Avanzadas (LMA), Universidad de Zaragoza, 50018 Zaragoza, Spain
3
Fundación ARAID, 50018 Zaragoza, Spain
*
Authors to whom correspondence should be addressed.
These authors contributed equal to this work.
Academic Editors: Si Wu and Sarah Perrett
Biomolecules 2022, 12(4), 594; https://doi.org/10.3390/biom12040594
Received: 13 March 2022 / Revised: 8 April 2022 / Accepted: 14 April 2022 / Published: 18 April 2022
(This article belongs to the Special Issue Single-Molecule Protein Dynamics)
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. View Full-Text
Keywords: adhesion maps; atomic force microscopy; jumping mode; molecular recognition imaging; rupture force; protein:ligand interactions; single molecule; protein detection adhesion maps; atomic force microscopy; jumping mode; molecular recognition imaging; rupture force; protein:ligand interactions; single molecule; protein detection
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MDPI and ACS Style

Marcuello, C.; de Miguel, R.; Lostao, A. Molecular Recognition of Proteins through Quantitative Force Maps at Single Molecule Level. Biomolecules 2022, 12, 594. https://doi.org/10.3390/biom12040594

AMA Style

Marcuello C, de Miguel R, Lostao A. Molecular Recognition of Proteins through Quantitative Force Maps at Single Molecule Level. Biomolecules. 2022; 12(4):594. https://doi.org/10.3390/biom12040594

Chicago/Turabian Style

Marcuello, Carlos, Rocío de Miguel, and Anabel Lostao. 2022. "Molecular Recognition of Proteins through Quantitative Force Maps at Single Molecule Level" Biomolecules 12, no. 4: 594. https://doi.org/10.3390/biom12040594

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