Modification of major plasma proteins by acrylamide and glycidamide: Preliminary screening by nano liquid chromatography with tandem mass spectrometry

Abstract

Environmental and food-borne acrylamide is a suspected carcinogen in humans and is associated with several cancer types. Its biological metabolite, glycidamide, is also harmful to human health. The presence of acrylamide in the living environment makes this toxic chemical an important public health issue. Acrylamide and glycidamide bind with proteins to form protein adducts in metabolic processes. These metabolic adducts can be considered environmental modifications of proteins. This study used a simple proteomic strategy to identify acrylamide and glycidamide adducts bound in major plasma proteins. After simple sample preparation, new protein modifications by acrylamide and glycidamide were identified using nano LC combined with quadruple time-of-flight (Q-TOF) mass spectrometry. This method required only 10 μL of human plasma sample for protein modification survey. Hopefully, this strategy can help to discover protein-acrylamide (or glycidamide) adducts that are biomarkers of human exposure to high-dose acrylamide. These biomarkers may also elucidate the metabolic pathways of acrylamide and glycidamide.