Nutriproteomics: technologies and applications for identification and quantification of biomarkers and ingredients

Abstract

Nutrition refers to the process by which a living organism ingests and digests food and uses the nutrients therein for growth, tissue maintenance and all other functions essential to life. Food components interact with our body at molecular, cellular, organ and system level. Nutrients come in complex mixtures, in which the presence and concentration of single compounds as well as their interactions with other compounds and the food matrix influence their bioavailability and bioefficacy. Traditionally, nutrition research mainly concentrated on supplying nutrients of quality to nourish populations and on preventing specific nutrient deficiencies. More recently, it investigates health-related aspects of individual ingredients or of complete diets, in view of health promotion, performance optimisation, disease prevention and risk assessment. This review focuses on proteins and peptides, their role as nutrients and biomarkers and on the technologies developed for their analysis. In the first part of this review, we provide insights into the way proteins are currently characterised and analysed using classical and emerging proteomic approaches. The scope of the second part is to review major applications of proteomics to nutrition, from characterisation of food proteins and peptides, via investigation of health-related food benefits to understanding disease-related mechanisms.

Proteomics of major bovine milk proteins: Novel insights

“…This MS-based technique has been extensively applied in milk proteins. Up to seven of the major MFGM proteins have been absolutely quantified by MRM (Affolter, Grass, Vanrobaeys, Casado, & Kussmann, 2010;Fong & Norris, 2009;Sénéchal & Kussmann, 2011). Lutter, Parisod, and Weymuth (2011) developed an MRM assay to detect and quantify trace amounts of the four major milk proteins (e.g., α S2 -CN, β-CN, κ-CN and β-Lg) in different food products.…”

“…The general MS approaches cannot give a high discovery rate; PTMs are therefore required to be purified and enriched (Szabo & Janaky, 2011). Several methods have been applied for the enrichment of phosphorylated (e.g., anti-phosphoserine antibodies, immobilised metal affinity chromatography, and chemical modification and strong anion exchange chromatography) and glycosylated proteins (e.g., cell surface capture technology or affinity with lectins) (Sénéchal & Kussmann, 2011). Nevertheless, the non-specific binding capacity of certain amino acids such as Asp and Glu lowers the selectivity of some enrichment methods.…”

Structural aspects of legume proteins and nutraceutical properties

“…These properties resemble those previously ascribed to peptides isolated from milk and dairy products, as well as to those from other animal -fish, meat, egg foods. Peptides of different sizes and even intact plant proteins, especially those from protein-rich seeds, such as legumes, have been shown to exert various beneficial effects in humans, notably in bone and cardiovascular health, inflammation, cancer prevention, weight control, insulin sensitivity, immune cell activity, and mineral absorption (Carbonaro, 2011;Jahan-Mihan, Luhovyy, Khoury, & Anderson, 2011;Rebello, Greenway, & Finley, 2014;Senechal & Kussmann, 2011). Several proteins and peptides from legume seeds can now be included into the category of "nutraceuticals" (or "functional components").…”

The Role of Clinical Proteomics, Lipidomics, and Genomics in the Diagnosis of Alzheimer’s Disease

“…Clinical biomarker discoveries have become important with nutriproteomics [154,155,156] as a technology that could determine biomarkers that may assist with the maintenance of normal cognitive development in individuals at risk of AD. The ingestion of nutrients allows proteomic tools to characterize molecular and cellular changes in protein expression and function in the plasma and CSF [157,158,159,160] with respect to nutritional diets that activate the anti-aging gene Sirt 1 and allow proteins such as amyloid beta/alpha synuclein to maintain monomer interactions and prevent self-association that induces inflammation [38,39].…”