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Decoupling competing surface binding kinetics and reconfiguration of receptor footprint for ultrasensitive stress assays.
- Source :
-
Nature nanotechnology [Nat Nanotechnol] 2015 Oct; Vol. 10 (10), pp. 899-907. Date of Electronic Publication: 2015 Aug 17. - Publication Year :
- 2015
-
Abstract
- Cantilever arrays have been used to monitor biochemical interactions and their associated stress. However, it is often necessary to passivate the underside of the cantilever to prevent unwanted ligand adsorption, and this process requires tedious optimization. Here, we show a way to immobilize membrane receptors on nanomechanical cantilevers so that they can function without passivating the underlying surface. Using equilibrium theory, we quantitatively describe the mechanical responses of vancomycin, human immunodeficiency virus type 1 antigens and coagulation factor VIII captured on the cantilever in the presence of competing stresses from the top and bottom cantilever surfaces. We show that the area per receptor molecule on the cantilever surface influences ligand-receptor binding and plays an important role on stress. Our results offer a new way to sense biomolecules and will aid in the creation of ultrasensitive biosensors.
- Subjects :
- Animals
Anti-Bacterial Agents metabolism
Camelids, New World
Equipment Design
Factor VIII metabolism
HIV-1 immunology
Humans
Kinetics
Models, Molecular
Protein Binding
Single-Domain Antibodies immunology
Surface Plasmon Resonance instrumentation
Surface Properties
Vancomycin metabolism
env Gene Products, Human Immunodeficiency Virus immunology
Immobilized Proteins metabolism
Receptors, Cell Surface metabolism
Surface Plasmon Resonance methods
Subjects
Details
- Language :
- English
- ISSN :
- 1748-3395
- Volume :
- 10
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- Nature nanotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 26280409
- Full Text :
- https://doi.org/10.1038/nnano.2015.174