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A simplified biomolecule attachment strategy for biosensing using a porous Si oxide interferometer
Author(s) -
Perelman Loren A.,
Schwartz Michael P.,
Wohlrab Aaron M.,
VanNieuwenhze Michael S.,
Sailor Michael J.
Publication year - 2007
Publication title -
physica status solidi (a)
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.532
H-Index - 104
eISSN - 1862-6319
pISSN - 1862-6300
DOI - 10.1002/pssa.200674360
Subject(s) - biomolecule , bioconjugation , bovine serum albumin , covalent bond , biosensor , chemistry , peptide , linker , adsorption , alanine , molecule , matrix (chemical analysis) , lysine , combinatorial chemistry , oxide , nanotechnology , materials science , chromatography , organic chemistry , amino acid , biochemistry , computer science , operating system
A simple strategy for linking biomolecules to porous Si surfaces and detecting peptide/drug binding is described. Porous Si is prepared using an electrochemical etch and then thermally oxidized by heating in ambient atmosphere. Bovine serum albumin (BSA) is then non‐covalently adsorbed to the inner pore walls of the porous Si oxide (PSiO 2 ) matrix. The BSA layer is used as a linker for covalent attachment of the peptide Ac‐L‐Lysine‐D‐Alanine‐D‐Alanine (KAA) using published bioconjugation chemistry. BSA‐coated surfaces functionalized with KAA display specificity for the glycopeptide vancomycin while resisting adsorption of non‐specific reagents. While the biomolecule attachment strategy reported here is used to bind peptides, the scheme can be generalized to the linking of any primary amine‐containing molecule to PSiO 2 surfaces. (© 2007 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)