Labeling primary amine groups in peptides and proteins with N-hydroxysuccinimidyl ester modified Fe3O4@SiO2 nanoparticles containing cleavable disulfide-bond linkers.

ABSTRACT: The surface of superparamagnetic silica coated iron oxide (Fe3O4@SiO2) nanoparticles was functionalized with a disulfide bond linked N-hydroxysuccinimidyl (NHS) ester group in order to develop a method for labeling primary amines in peptides/proteins. The nanoparticle labeled proteins/peptides formed after NHS ester reaction with the primary amine groups were isolated using a magnet without any additional purification step. Nanoparticle moieties conjugated to peptides/proteins were then trimmed by cleavage at the disulfide linker with a reducing agent. The labeled peptides were analyzed by LC-MS/MS to determine their sequences and the sites of NHS ester labeling. This novel approach allowed characterization of lysine residues on the solvent accessible surface of native bovine serum albumin

SUBMITTER: Patil US 

PROVIDER: S-EPMC3865927 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature