Journal article
Optimization of Localized Surface Plasmon Resonance Transducers for Studying Carbohydrate-Protein Interactions
Analytical Chemistry, Vol.84(1), pp.232-240
Jan/2012
Abstract
Noble metal nanostructures supporting localized surface plasmons (SPs) have been widely applied to chemical and biological sensing. Changes in the refractive index near the nanostructures affect the SP extinction band, making localized surface plasmon resonance (LSPR) spectroscopy a convenient tool for studying biological interactions. Carbohydrate-protein interactions are of major importance in living organisms; their study is crucial for understanding of basic biological processes and for the construction of biosensors for diagnostics and drug development. Here LSPR transducers based on gold island films prepared by evaporation on glass and annealing were optimized for monitoring the specific interaction between Concanavalin A (Con A) and D-(+)-mannose. The sugar was modified with a PEG-thiol linker and immobilized on the Au islands. Sensing assays were performed under stationary and flow conditions, the latter providing kinetic parameters for protein binding and dissociation. Ellipsometry and Fourier transform-infrared (FT-IR) data, as well as scanning electron microscopy (SEM) imaging of fixated and stained samples, furnished independent evidence for the protein-sugar recognition. Enhanced response and visual detection of protein binding was demonstrated using Au nanoparticles stabilized with the linker-modified mannose molecules. Mannose-coated transducers display an excellent selectivity toward Con A in the presence of a large excess of bovine serum albumin (BSA).
Details
- Title
- Optimization of Localized Surface Plasmon Resonance Transducers for Studying Carbohydrate-Protein Interactions
- Creators
- Giuliano Bellapadrona (null) - The Weizmann Institute of ScienceAlexander B. Tesler (null)Dan Gruenstein (null)Laila H. Hossain (null)Raghavendra Kikkeri (null)Peter H. Seeberger (null)Alexander Vaskevich (null) - The Weizmann Institute of ScienceIsrael Rubinstein (null) - The Weizmann Institute of Science
- Resource Type
- Journal article
- Publication Details
- Analytical Chemistry, Vol.84(1), pp.232-240; Jan/2012
- Number of pages
- 9
- Language
- English
- DOI
- https://doi.org/10.1021/ac202363t
- Grant note
- Israel Science Foundation [1251/11]; Schmidt Minerva Center on Supramolecular Architectures; Max-Planck Society; European UnionG.B., A.B.T., and D.G. contributed equally to this work. AV. and I.R. acknowledge support of this work by the Israel Science Foundation, Grant No. 1251/11, and by the Schmidt Minerva Center on Supramolecular Architectures. The electron microscopy studies were conducted at the Irving and Cherna Moskowitz Center for Nano and Bio-Nano Imaging, Weizmann Institute of Science. This research is made possible in part by the historic generosity of the Harold Perlman family. P.H.S. and D.G. thank the Max-Planck Society and the European Union FP7 (CARMUSYS) for financial support. Generous financial support by the Korber Foundation is gratefully acknowledged._ALMAME_DELIMITER_
- Record Identifier
- 993267467103596
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