Novel tertiary amine oxide surfaces that resist nonspecific protein adsorption.
Novel surfaces derivatized with tertiary amine oxides have been prepared and tested for their ability to resist nonspecific protein adsorption. The oxidation of tertiary amines supported on triazine units was carried out using mCPBA to give a format allowing conjugation of biologically active ligands alongside them. Adsorption to these surfaces was tested and compared to adsorption to a set of commercial and custom oligo-/poly(ethylene glycol) (OEG/PEG) supports by challenging them with a protein display library presented on bacteriophage lambda. The new class of amine oxide surfaces is found to compare favorably with the performance of the OEG/PEG supports in the prevention of nonspecific binding.
Dilly
Suzanne J
SJ
Department of Chemistry, University of Warwick, Coventry, UK.
Beecham
Matthew P
MP
Brown
Steven P
SP
Griffin
John M
JM
Clark
Andrew J
AJ
Griffin
Craig D
CD
Marshall
Jacqueline
J
Napier
Richard M
RM
Taylor
Paul C
PC
Marsh
Andrew
A
D000327:Adsorption; D000588:Amines / Q000737:chemistry*; D008024:Ligands; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010087:Oxides / Q000737:chemistry*; D011092:Polyethylene Glycols / Q000737:chemistry; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry*; D013499:Surface Properties; D014227:Triazines / Q000737:chemistry
D000588:Amines; D008024:Ligands; D010087:Oxides; D011506:Proteins; D014227:Triazines; D011092:Polyethylene Glycols