Functionalized xenon as a biosensor.

M M Spence; S M Rubin; I E Dimitrov; E J Ruiz; D E Wemmer; A Pines; S Q Yao; F Tian; P G Schultz

doi:10.1073/pnas.191368398

Home/Archive/PubMed

PubMed · 11535830

Functionalized xenon as a biosensor.

M M Spence·S M Rubin·I E Dimitrov·E J Ruiz·D E Wemmer·A Pines·S Q Yao·F Tian·P G Schultz

View original source ↗Export metadata ↓

Abstract

The detection of biological molecules and their interactions is a significant component of modern biomedical research. In current biosensor technologies, simultaneous detection is limited to a small number of analytes by the spectral overlap of their signals. We have developed an NMR-based xenon biosensor that capitalizes on the enhanced signal-to-noise, spectral simplicity, and chemical-shift sensitivity of laser-polarized xenon to detect specific biomolecules at the level of tens of nanomoles. We present results using xenon "functionalized" by a biotin-modified supramolecular cage to detect biotin-avidin binding. This biosensor methodology can be extended to a multiplexing assay for multiple analytes.

Explore related subjects

Avidin Biosensing Techniques Biotin Nuclear Magnetic Resonance, Biomolecular Proteins Xenon Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

Keep this discovery

Explore connections, maps & timelines

BibTeX RIS

M M Spence, S M Rubin, I E Dimitrov, E J Ruiz, D E Wemmer, A Pines, S Q Yao, F Tian, P G Schultz. 2001-09-04. Functionalized xenon as a biosensor.. https://doi.org/10.1073/pnas.191368398

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed2003

Use of water-dispersible Fe(2)O(3) nanoparticles with narrow size distributions in isolating avidin.

Synthetic approaches that vigorously control the microstructures of water-dispersible gamma-Fe(2)O(3) nanoparticles such as size and size uniformity are of importance to the potential biological applications of these nanomaterials. In the present paper, water-dispersible gamma-Fe(2)O(3) nanocrystals with narrow size distributions (bipy-Fe(2)O(3)) were prepared via a site-exchange reaction. These particular materials are superparamagnetic and stable within a wide range of pH. Introduction of the biotin functionality onto the surfaces of bipy-Fe(2)O(3) enabled the affinity isolation of the protein avidin from its incubation solution magnetically with 96% efficiency.

Avidin↗

PubMed2003

Synthesis and characterization of thermoreversible biopolymer microgels based on hydrogen bonded nucleobase pairing.

We describe the synthesis and characterization of a thermoreversibly cross-linked biopolymer microgel based on protein, DNA, and peptide nucleic acid (PNA) components. The DNA assembles into a trifunctional three-way junction (TWJ) with single-stranded overhangs. PNA oligomers complementary to these overhangs and bearing terminal biotin groups hybridize to the DNA TWJ and simultaneously bind to the tetrafunctional protein avidin, leading to a cross-linked system. Dynamic light scattering experiments reveal that micron-sized particles are formed. Static light scattering was used to characterize the internal structure of these microgels, which were found to have a fractal dimension of 1.85, indicative of a loose network structure. Heating disrupts the weakest component in the system, namely the PNA-DNA hybrid, resulting in dissolution of the microgel, while cooling restores the hydrogen bonding leading to reassembly of the microgel. Variation of the nucleotide sequence permits tuning of the gelation temperature with fine control.

Avidin↗

PubMed2003

A single-channel sensor based on gramicidin controlled by molecular recognition at bilayer lipid membranes containing receptor.

A novel ion-channel sensor based on a membrane bound receptor and a single gramicidin channel is described, in which the binding of an analyte to the membrane bound receptor modulates the single-channel activity of gramicidin. The sensor is composed of a planar bilayer lipid membrane (BLM) containing biotin-labeled phosphatidylethanolamine as receptor for avidin and gramicidin as signal transducer. When the receptor catches an analyte (avidin or ferritin-labeled avidin (FA)) at the membrane surface, the bilayer structure is locally distorted and the gramicidin monomer/dimer kinetics is modulated in a manner that the fraction of channel opening with a short lifetime ( < or = 100 ms) to the total opening events increases. The fraction was found to increase with the concentration of avidin from 1.0 x 10(-9) to 1.0 x 10(-6) M and of FA from 1.0 x 10(-9) to 1.0 x 10(-8) M. With dinitrophenyl-labeled PE embedded as receptor in the BLM for monoclonal anti-dinitrophenyl antibody (anti-DNP), the fraction of channel openings ( < or = 100 ms) increased with the concentration of anti-DNP from 2.0 x 10(-9) to 2.0 x 10(-7) g/ml. Bovine serum albumin (BSA) and anti-BSA antibody caused no changes in the channel opening. The possible mechanism of analyte-induced modulation of single-channel activity of gramicidin is also discussed.

Avidin↗