Covalently modified silicon and diamond surfaces: resistance to nonspecific protein adsorption and optimization for biosensing.
We report the direct covalent functionalization of silicon and diamond surfaces with short ethylene glycol (EG) oligomers via photochemical reaction of the hydrogen-terminated surfaces with terminal vinyl groups of the oligomers, and the use of these monolayers to control protein binding at surfaces. Photochemical modification of Si(111) and polycrystalline diamond surfaces produces EG monolayers linked via Si-C bond formation (silicon) or C-C bond formation (diamond). X-ray photoelectron spectroscopy was used to characterize the monolayer composition. Measurements using fluorescently labeled proteins show that the EG-functionalized surfaces effectively resist nonspecific adsorption of proteins. Additionally, we demonstrate the use of mixed monolayers on silicon and diamond and apply these surfaces to control specific versus nonspecific binding to optimize a model protein sensing assay.
Department of Chemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.
Tami L
TL
Lasseter
Brian H
BH
Clare
Nicholas L
NL
Abbott
Robert J
RJ
Hamers
D000327:Adsorption; D000588:Amines / Q000737:chemistry; D001360:Avidin / Q000032:analysis / Q000737:chemistry; D015374:Biosensing Techniques / Q000379:methods*; D002364:Caseins / Q000032:analysis / Q000737:chemistry; D018130:Diamond / Q000737:chemistry*; D005026:Ethylene Glycols / Q000737:chemistry; D005340:Fibrinogen / Q000032:analysis / Q000737:chemistry; D011506:Proteins / Q000032:analysis / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000032:analysis / Q000737:chemistry; D012825:Silicon / Q000737:chemistry*; D013050:Spectrometry, Fluorescence; D013499:Surface Properties; D013816:Thermodynamics
D000588:Amines; D002364:Caseins; D005026:Ethylene Glycols; D011506:Proteins; D001360:Avidin; D012710:Serum Albumin, Bovine; D018130:Diamond; D005340:Fibrinogen; D012825:Silicon