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International audience; This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.

International audience; In the elderly, oral functions are modified by changes in muscular force or saliva production among others, resulting in inadequate food fragmentation which potentially impacts on oral and gastrointestinal digestion. The purpose of this work was to evaluate the consequences of oral deficiencies on the starch and protein digestibility of bread. In vitro boluses were prepared with the AM 2 masticator using normal and deficient mastication programming. Normal mastication (NM) and deficient mastication in terms of force (DfM), saliva (DsM), and their combination (DfsM) were performed. Static in vitro digestion, simulating physiological conditions in the elderly, were carried out. Bolus particle size, starch and protein digestibility, Fourier-transform infrared (FTIR) spectroscopy, and microstructure after in vitro oral and gastrointestinal digestion were analysed. More compacted boluses were observed after deficient mastication combined with greater particle sizes. The poorly fragmented boluses obtained with deficient mastication affected the oral digestion of starch, probably due to lower saliva impregnation. Digesta from deficient mastication boluses exhibited lower D-glucose release and degree of protein hydrolysis. FTIR results in the carbohydrates region also revealed weaker initiation of oral digestion of starch in DsM and DfsM boluses. These results on bread demonstrate for the first time how oral deficiencies modify nutrient bioaccessibility and, therefore, stress the importance of designing foods for specific populations such as the elderly.

Apolipoprotein E (ApoE) has become a primary focus of research after the discovery of its strong linkage to Alzheimer&rsquo, s disease (AD), where the ApoE4 variant is the highest genetic risk factor for this disease. ApoE is commonly found in amyloid deposits of different origins, and its interaction with amyloid-&beta, peptide (A&beta, ), the hallmark of AD, is well known. However, studies on the interaction of ApoEs with other amyloid-forming proteins are limited. Islet amyloid polypeptide (IAPP) is an amyloid-forming peptide linked to the development of type-2 diabetes and has also been shown to be involved in AD pathology and vascular dementia. Here we studied the impact of ApoE on IAPP aggregation and IAPP-induced toxicity on blood vessel pericytes. Using both in vitro and cell-based assays, we show that ApoE efficiently inhibits the amyloid formation of IAPP at highly substoichiometric ratios and that it interferes with both nucleation and elongation. We also show that ApoE protects the pericytes against IAPP-induced toxicity, however, the ApoE4 variant displays the weakest protective potential. Taken together, our results suggest that ApoE has a generic amyloid-interfering property and can be protective against amyloid-induced cytotoxicity, but there is a loss of function for the ApoE4 variant.