Decoupling competing surface binding kinetics and reconfiguration of receptor footprint for ultrasensitive stress assays

TY - JOUR

T1 - Decoupling competing surface binding kinetics and reconfiguration of receptor footprint for ultrasensitive stress assays

AU - Patil, Samadhan B.

AU - Vögtli, Manuel

AU - Webb, Benjamin

AU - Mazza, Giuseppe

AU - Pinzani, Massimo

AU - Soh, Yeong Ah

AU - McKendry, Rachel A.

AU - Ndieyira, Joseph W.

PY - 2015/8/17

Y1 - 2015/8/17

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84943357285&partnerID=8YFLogxK

U2 - 10.1038/nnano.2015.174

DO - 10.1038/nnano.2015.174

M3 - Article

C2 - 26280409

AN - SCOPUS:84943357285

SN - 1748-3387

VL - 10

SP - 899

EP - 907

JO - Nature Nanotechnology

JF - Nature Nanotechnology

IS - 10

ER -