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Docking of a Second Functional Protein Layer to a Streptavidin Matrix on a Solid Support: Studies with a Quartz Crystal Microbalance
Author(s) -
Müller Wolfgang,
Ringsdorf Helmut,
Suci Peter,
Herron James N.,
Ebato Hiroshi,
Okahata Yoshio
Publication year - 1992
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199210871
Subject(s) - quartz crystal microbalance , streptavidin , biotinylation , chemistry , matrix (chemical analysis) , quartz , layer (electronics) , materials science , crystallography , analytical chemistry (journal) , biophysics , chromatography , chemical engineering , adsorption , nanotechnology , biotin , biochemistry , organic chemistry , composite material , biology , engineering
A long, flexible, hydrophilic spacer is needed in the biotinlipid for the specific binding of the protein streptavidin to the lipid‐containing membrane. This was shown by measurements with a quartz crystal microbalance, which indicated that 1 was specifically binding. The binding of a second protein layer of biotinylated Fab fragment to the streptavidin matrix could also be monitored in real time by this method.