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LC-MS/MS analysis on in-vivo mice gastrointestinal digests

ABSTRACT: Food protein amyloid fibrils have superior technological,nutritional,sensorial,and physical properties compared to native monomers, butthere is yet insufficient understanding of their digestive fate and safety for wide consumption.By combining SDS,ELISA,fluorenscence,AFM, MALDI-MS, CD microfluidics,and SAXS techniques for the characterization of blg and lysozyme amyloid fibrils subjected to in-vitro gastrointestinal digestion.LC-MS/MS analysis on the fate of blg/lysozyme amyloid fibrils digested in vivo by mice was applied to verify our in vitro results.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Blood Serum, Intestinal Juice, Colon

SUBMITTER: Dan Xu

LAB HEAD: Raffaele Mezzenga

PROVIDER: PXD045698 | Pride | 2023-10-30

REPOSITORIES: Pride

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			Action	DRS
	colon_blg_fibril_1.raw	Raw
	colon_blg_fibril_2.raw	Raw
	colon_blg_fibril_3.raw	Raw
	colon_blg_fibril_4.raw	Raw
	colon_blg_fibril_5.raw	Raw

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Publications

Food amyloid fibrils are safe nutrition ingredients based on in-vitro and in-vivo assessment.

Xu Dan D Zhou Jiangtao J Soon Wei Long WL Kutzli Ines I Molière Adrian A Diedrich Sabine S Radiom Milad M Handschin Stephan S Li Bing B Li Lin L Sturla Shana J SJ Ewald Collin Y CY Mezzenga Raffaele R

Nature communications 20231026 1

Food protein amyloid fibrils have superior technological, nutritional, sensorial, and physical properties compared to native monomers, but there is as yet insufficient understanding of their digestive fate and safety for wide consumption. By combining SDS-PAGE, ELISA, fluorescence, AFM, MALDI-MS, CD, microfluidics, and SAXS techniques for the characterization of β-lactoglobulin and lysozyme amyloid fibrils subjected to in-vitro gastrointestinal digestion, here we show that either no noticeable c ...[more]

PMID: 37884488

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Project description:Amyloid fibrils are polymeric structures originating from aggregation of misfolded proteins. In vivo, proteolysis may modulate amyloidogenesis and fibril stability. In light chain (AL) amyloidosis, fragmented light chains (LCs) are abundant components of amyloid deposits; however, site and timing of proteolysis are debated. Identification of the N- and C-termini of LC fragments is instrumental to understanding involved processes and enzymes. We investigated the N- and C-terminome of the LC proteoforms in fibrils extracted from the hearts of two AL cardiomyopathy patients, using a proteomic approach based on derivatization of N- and C-terminal residues, followed by mapping of fragmentation sites on the structures of native and fibrillar relevant LCs. We provide the first high-specificity map of proteolytic cleavages in natural AL amyloid. Proteolysis occurs both on the LCs’ variable and constant domains, generating a complex fragmentation pattern. The structural analysis indicates extensive remodeling, by multiple proteases, largely taking place on poorly folded regions of the fibril surfaces. This study adds novel important knowledge on amyloid LCs processing: although our data do not exclude that proteolysis of native LC dimers may destabilize their structure and favor fibril formation, they show that LC deposition largely precedes the proteolytic events documentable in mature AL fibrils.

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