Bioavailability and Health Impact of Ingested Amyloid‐like Protein Fibrils and their Link with Inflammatory Status: A Need for More Research?

Abstract

The use of amyloid‐like protein fibrils (ALFs) in food formulations looks very promising in terms of improving techno‐functional properties, but raises some concerns in terms of food safety, because of their structural resemblance to disease‐related endogenous amyloids. This review focuses on the biological fate and potential health implications of ingested ALF structures in both healthy and predisposed individuals. A comprehensive overview of ALF gastrointestinal digestion, intestinal absorption, and systemic dissemination is provided, in addition to a thorough assessment of potential ALF cross‐seeding of endogenous precursor proteins linked to (non)neurodegenerative amyloidosis. In general, this study concludes that the health impact of ALF consumption remains widely understudied and merits additional research efforts to determine the exact extent to which ALF ingestion may influence the general health status.

Nanofibrils of food‐grade proteins: Formation mechanism, delivery systems, and application evaluation

“…In contrast, others proved FGPNs were more susceptible to digestion due to the (partial) unfolding of proteins during fibrillation resulting in higher exposure of peptide bonds (Nyemb et al., 2014). The digestive behavior of FGPNs was also influenced by the food matrix and gastrointestinal environment, involving individual differences and fed/fasted conditions (Luyckx et al., 2022). Next, we discussed the digestive behavior of FGPNs under complex gastrointestinal conditions; we believed FGPNs were easy to digest and lost their fibrous structure.…”

“…In general, adding preformed nanofibrils for the same proteins is called seeding, whereas the process that occurs between two different source proteins is defined as cross‐seeding (Hao et al., 2019). A more important problem is the risk of the cross‐seeding of endogenous proteins by food‐derived fibril fragments and fibril cores (Luyckx et al., 2022). The link between functional and pathological amyloid fibrils in the body may increase the tendency to mutually aggregate, greatly increasing the potential health risk of accelerating pathological protein precursors to fibrillation after exogenous FGPNs enter the body.…”

“…Although previous studies have shown that β‐lg nanofibrils can be reformed after 180 min incubation under gastric conditions (Bateman et al., 2011). Maintaining a pH 1.2 is key to triggering the reaction, which is extremely low, even in fasted conditions (Luyckx et al., 2022).…”

“…However, animal models including genetically predisposed and inflammatory‐stimulated mice have been shown to accumulate pathological amyloid deposits in many organs when fed high doses of foie gras amyloids (Solomon et al., 2007). It was reported that a variety of disease‐related endogenous proteins in the body are susceptible to amyloid formation as a result of aging, inflammation, or genetic mutations (Luyckx et al., 2022). This undoubtedly increases the concern of specific susceptible populations for cross‐seeding of food‐derived amyloid.…”

Amyloid-like Aggregation of Wheat Gluten and Its Components during Cooking: Mechanisms and Structural Characterization

“…Unlike pathologically acquired amyloid fibrils, which have been linked to the onset of neurodegenerative diseases, food-borne amyloid-like fibrils (AFs), despite sharing a cross-β sheet structure with the former, have not been associated with such pathogenic effects. , Consequently, they have garnered significant attention in recent research endeavors. Emerging studies aim to unveil the intriguing self-assembly behaviors of proteins inherent to food-borne AFs, differentiating them from conventional aggregation phenomena .…”