Journal article
Reduction of nonspecific protein adsorption on cantilever biosensors caused by transverse resonant mode vibration
Analyst (London), v 139(5), pp 1112-1120
07 Mar 2014
PMID: 24416758
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
We examine if vibration of millimeter-sized cantilever sensors can release nonspecifically adsorbed proteins. Integrated electrochemical and mass-change measurement as well as fluorescence assays showed transverse surface vibration released nonspecifically bound proteins in samples prepared at 0.2-3.6 mg bovine serum albumin (BSA) per mL. Extent of release was directly related to magnitude of excitation voltage (Vex) applied to the self-actuating lead zirconate titanate (PZT) cantilever over three log units (0, 10 mV, 100 mV, and 1 V). Vibration-induced release was not instantaneous, but had an apparent first-order rate constant (kapp) which ranged from 0.02-0.1 min(-1). Results suggest significant serum albumin protein release could be achieved using excitation voltages of 1 V in millimeter-sized cantilever sensors. Complementary experiments with thiolated DNA, which binds to surface gold 〈111〉 sites with ∼ four times higher binding energy than BSA, showed negligible release under the same vibration magnitude. The results of the study suggest a direct correlation between surface-adsorbate binding energy and the effectiveness of vibration-induced release. We suggest that the release mechanism includes contributions from surface strain energy, body force, and acoustic streaming-associated hydrodynamic effects. The primary contribution of this study suggests that surface vibration of cantilever sensors may be useful in reducing nonspecific adsorption, especially for biosensing of analytes present in a complex background.
Metrics
Details
- Title
- Reduction of nonspecific protein adsorption on cantilever biosensors caused by transverse resonant mode vibration
- Creators
- Blake N Johnson - Department of Chemical and Biological Engineering, Drexel University, Philadelphia, PA 19104, USA. mutharasan@drexel.eduRaj Mutharasan
- Publication Details
- Analyst (London), v 139(5), pp 1112-1120
- Publisher
- Royal Society of Chemistry; England
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Chemical and Biological Engineering
- Web of Science ID
- WOS:000330778400031
- Scopus ID
- 2-s2.0-84893277888
- Other Identifier
- 991014877782404721
UN Sustainable Development Goals (SDGs)
This publication has contributed to the advancement of the following goals:
InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Chemistry, Analytical