Molecular Recognition of Avidin on Biotin-Functionalized Gold Surfaces Detected by FT-IRRAS and Use of Metal Carbonyl Probes

Fourier transform infrared reflection-absorption spectroscopy (FT-IRRAS) was successively used to monitor the covalent immobilization of biotin molecules onto a planar gold substrate covered with a self-assembled monolayer of cystamine and to transduce the molecular recognition of avidin and biotin....

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Published inJournal of colloid and interface science Vol. 245; no. 1; pp. 204 - 207
Main Authors Yam, Chi-Ming, Pradier, Claire-Marie, Salmain, Michèle, Fischer-Durand, Nathalie, Jaouen, Gérard
Format Journal Article
LanguageEnglish
Published San Diego, CA Elsevier Inc 01.01.2002
Elsevier
Subjects
Analytical biochemistry: general aspects, technics, instrumentation
Analytical chemistry
Analytical, structural and metabolic biochemistry
avidin
Avidin - chemistry
Biological and medical sciences
biotin
Biotin - chemistry
Chemical Sciences
Enzymes, Immobilized - chemistry
Fourier transform infrared reflection-absorption spectroscopy
Fundamental and applied biological sciences. Psychology
Gold - chemistry
Material chemistry
molecular recognition
Molecular Structure
Organometallic Compounds - chemistry
Protein Binding
Sensitivity and Specificity
Spectroscopy, Fourier Transform Infrared
Surface Properties
molecular recognition
Fourier transform infrared reflection-absorption spectroscopy
avidin
biotin
Molecular recognition
Biotin
Avidin
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Summary:Fourier transform infrared reflection-absorption spectroscopy (FT-IRRAS) was successively used to monitor the covalent immobilization of biotin molecules onto a planar gold substrate covered with a self-assembled monolayer of cystamine and to transduce the molecular recognition of avidin and biotin. This detection was greatly facilitated and made selective by the labeling of avidin and of biotin with various transition metal carbonyl probes. The binding of avidin to the surface was optimized by blocking the nonspecific binding sites by adsorption of an unrelated protein, bovine serum albumin. This work exemplifies the feasibility of detecting biomolecular associations involving molecules of any size at a liquid/solid interface by using a simple and accessible surface analysis technique.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0021-9797
1095-7103
DOI:10.1006/jcis.2001.7981