Detecting the chemoselective ligation of peptides to silicon with the use of cobalt-carbonyl labels.
While fluorescent-based methods are generally used to detect the immobilization and the interactions of biomolecules to solid supports, recent studies have shown their limitations in the case of silicon surfaces. As an alternative, we investigated the synthesis of peptides labeled with a metal transition complex and their subsequent immobilization to the silicon surfaces. The feasibility of using such probes has been explored by Fourier transform infrared spectroscopy (FTIR) and X-ray photoelectron spectroscopy (XPS). By starting with hydrogen-terminated or oxidized silicon surfaces, we functionalized those surfaces with semicarbazide groups and showed the site-specific linkage of glyoxylyl peptides labeled with a Co2(CO)6 moiety.
Olivier
Christophe
C
UMR CNRS 8161, Biological Institute of Lille, 1 rue du Professeur Calmette, 59021 Lille, France.
Perzyna
Aurore
A
Coffinier
Yannick
Y
Grandidier
Bruno
B
Stiévenard
Didier
D
Melnyk
Oleg
O
Durand
Jean-Olivier
JO
D003035:Cobalt / Q000737:chemistry*; D006859:Hydrogen / Q000737:chemistry*; D010084:Oxidation-Reduction; D010455:Peptides / Q000737:chemistry*; D012825:Silicon / Q000737:chemistry*; D013052:Spectrometry, X-Ray Emission; D017550:Spectroscopy, Fourier Transform Infrared
D010455:Peptides; D003035:Cobalt; D006859:Hydrogen; D012825:Silicon