Dataset Information

Amino Acid Profiling with Chemometric Analysis as a Feasible Tool for the Discrimination of Marine-Derived Peptide Powders.

ABSTRACT: Marine-derived peptide powders have suffered from adulteration via the substitution of lower-price peptides or the addition of adulterants in the market. This study aims to establish an effective approach for the discrimination and detection of adulterants for four representative categories of marine-derived peptide powders, namely, oyster peptides, sea cucumber peptides, Antarctic krill peptides, and fish skin peptides, based on amino acid profiling alongside chemometric analysis. The principal component analysis and orthogonal partial least squares discriminant analysis results indicate that four categories of marine-derived peptides could be distinctly classified into four clusters and aggregated with the respective raw materials. Taurine, glycine, lysine, and protein contents were the major discriminants. A reliable classification model was constructed and validated by the prediction dataset, mixture sample dataset, and unclassified sample dataset with accuracy values of 100%, 100%, and 100%, respectively.

SUBMITTER: Wang Q

PROVIDER: S-EPMC8229220 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature

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Amino Acid Profiling with Chemometric Analysis as a Feasible Tool for the Discrimination of Marine-Derived Peptide Powders.

Wang Qin Q Wang Yanchao Y Jiang Xiaoming X Ma Lei L Li Zhaojie Z Chang Yaoguang Y Wang Yuming Y Xue Changhu C

Foods (Basel, Switzerland) 20210604 6

Marine-derived peptide powders have suffered from adulteration via the substitution of lower-price peptides or the addition of adulterants in the market. This study aims to establish an effective approach for the discrimination and detection of adulterants for four representative categories of marine-derived peptide powders, namely, oyster peptides, sea cucumber peptides, Antarctic krill peptides, and fish skin peptides, based on amino acid profiling alongside chemometric analysis. The principal ...[more]

PMID: 34199884

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Project description:ObjectiveGlucagon-like peptide-2 (GLP-2) is co-secreted with GLP-1 from gut endocrine cells, and both peptides act as growth factors to expand the surface area of the mucosal epithelium. Notably, GLP-2 also enhances glucose and lipid transport in enterocytes; however, its actions on control of amino acid (AA) transport remain unclear. Here we examined the mechanisms linking gain and loss of GLP-2 receptor (GLP-2R) signaling to control of intestinal amino acid absorption in mice.MethodsAbsorption, transport, and clearance of essential AAs, specifically lysine, were measured in vivo by Liquid Chromatography triple quadrupole Mass Spectrometry (LC-MS/MS) and ex vivo with Ussing chambers using intestinal preparations from Glp2r+/+ and Glp2r-/- mice. Immunoblotting determined jejunal levels of protein components of signaling pathways (PI3K-AKT, and mTORC1-pS6-p4E-BP1) following administration of GLP-2, protein gavage, and rapamycin to fasted Glp2r+/+ and Glp2r-/- mice. Expression of AA transporters from full thickness jejunum and 4F2hc from brush border membrane vesicles (BBMVs) was measured by real-time PCR and immunoblotting, respectively.ResultsAcute administration of GLP-2 increased basal AA absorption in vivo and augmented basal lysine transport ex vivo. GLP-2-stimulated lysine transport was attenuated by co-incubation with wortmannin, rapamycin, or tetrodotoxin ex vivo. Phosphorylation of mTORC1 effector proteins S6 and 4E-BP1 was significantly increased in wild-type mice in response to GLP-2 alone, or when co-administered with protein gavage, and abolished following oral gavage of rapamycin. In contrast, activation of GLP-1R signaling did not enhance S6 phosphorylation. Disruption of GLP-2 action in Glp2r-/- mice reduced lysine transport ex vivo and attenuated the phosphorylation of S6 and 4E-BP1 in response to oral protein. Moreover, the expression of cationic AA transporter slc7a9 in response to refeeding, and the abundance of 4F2hc in BBMVs following protein gavage, was significantly attenuated in Glp2r-/- mice.ConclusionsThese findings reveal an important role for GLP-2R signaling in the physiological and pharmacological control of enteral amino acid sensing and assimilation, defining an enteroendocrine cell-enterocyte axis for optimal energy absorption.

Dataset Information

Amino Acid Profiling with Chemometric Analysis as a Feasible Tool for the Discrimination of Marine-Derived Peptide Powders.

Publications

Amino Acid Profiling with Chemometric Analysis as a Feasible Tool for the Discrimination of Marine-Derived Peptide Powders.

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