Jun Ma’s research while affiliated with Shaanxi University of Science and Technology and other places

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Publications (4)


Figure 1. Hydrolyzed peptide segment distribution diagram. (a) Distribution of peptide lengths; (b) distribution of peptide activities; and (c) distribution of peptide source proteins.
Figure 3. Molecular docking diagrams of peptide segments with the DPP-IV enzyme. (a) Three-dimensional plan view and two-dimensional plan view of ILDKVGINY interaction with the DPP-IV enzyme. (b) The 3D plan view and 2D plan view of IPDKVGINY interaction with the DPP-IV enzyme. (c) Three-dimensional plan view of IIDKVGINY interaction with the DPP-IV enFigure 3. Molecular docking diagrams of peptide segments with the DPP-IV enzyme. (a) Threedimensional plan view and two-dimensional plan view of ILDKVGINY interaction with the DPP-IV enzyme. (b) The 3D plan view and 2D plan view of IPDKVGINY interaction with the DPP-IV enzyme. (c) Three-dimensional plan view of IIDKVGINY interaction with the DPP-IV enzyme. In the two-dimensional plan, the green dashed lines indicate hydrogen bonds, light green dashed lines indicate carbon-hydrogen bonds, and pink dashed lines indicate hydrophobic forces.
DPP-IV Inhibitory active peptide.
DPP-IV Inhibitory Peptide against In Vitro Gastrointestinal Digestion Derived from Goat’s Milk Protein and Its Activity Enhancement via Amino Acid Substitution
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August 2024

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12 Reads

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2 Citations

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Baoyuan He

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Yanhui Lian

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Haiyan Xue

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Yawen Wu

Goat milk protein can release a variety of bioactive peptides after digestion, while most of them are digested into free amino acids or dipeptides via the GI tract. We investigated the peptide profiles of goat milk protein following in vitro gastrointestinal digestion using LC-MS/MS and identified 683 bioactive peptides, including 105 DPP-IV inhibitory peptides. Among these peptides, ILDKVGINY (IL), derived from β-lactoglobulin, was found to be high in content and resistance to digestion. Herein, we explore the effect of amino acid residue substitution at the second N-terminus on its DPP-IV inhibitory activity. Three 9 polypeptide fragments (peptide IL, IP, and II) were synthesized and subjected to molecular docking and activity analysis. The peptide IL demonstrated the highest affinity for DPP-IV with a binding energy of −8.4 kcal/mol and a moderate IC50 value of 1.431 mg/mL determined based on the Caco-2 cell model. The replacement of specific amino acid residues by Pro and Leu led to an increase in the hydrophobic force interaction between the inhibitor peptide and DPP-IV. The inhibition rates of the three peptides were significantly different (p < 0.05). Peptide II containing an Ile residue instead of Leu resulted in a significant enhancement of DPP-IV inhibitory activity, with an IC50 value of 0.577 mg/mL. The GRAVY changes in the three peptides were consistent with the trend of the inhibitory rates. Therefore, the GRAVY of peptides and branch-chain amino acids should be considered in its activity improvement. The present study revealed the presence and activity of DPP-IV inhibitory peptides in goat milk, providing important insights for further investigation of their potential food functionality and health benefits.

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Identification of Immune-Active Peptides in Casein Hydrolysates and Its Transport Mechanism on a Caco-2 Monolayer

January 2023

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37 Reads

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8 Citations

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In this study, we investigated the transport mechanism of immune-active peptide fragments isolated from casein gastrointestinal hydrolysates via a Caco-2 monolayer. The casein gastrointestinal hydrolysates could stimulate B-lymphocyte proliferation and reduce the TNF-α level. Then, we identified the bioactive peptide fragments derived from casein gastrointestinal hydrolysis using LC-MS/MS. Our results demonstrated that the transport mechanism of five immune-active peptides at the cell level was bypass transport. In addition, the majority of peptide RYPLGYL was transported through the monolayer cell membrane as an intact form for playing immune-active functions. The KHPIK and FFSDK were mainly degraded into small fragments, except for a small amount passing through Caco-2 cells in an entire form. Overall, these results suggested that casein or its immune-active peptides might play a role in regulation of the intestinal immune system.


Citations (2)


... Bioactive peptides in mare milk have attracted more and more researchers' interest due to their diverse bioactivities. The most notable factors affecting these bioactive properties include chain length and amino acid sequence, with the amino acids at the termini being the most relevant for many reactions [26][27][28]. Studies have shown that heat treatment can increase the content of Glu, Asp, Met, and Cys in milk to varying degrees, increasing the frankincense flavor and improving the flavor of the product [29]. ...

Reference:

Peptidomic Analysis of Potential Bioactive Peptides in Mare Milk Under Different Heat Treatment Conditions
DPP-IV Inhibitory Peptide against In Vitro Gastrointestinal Digestion Derived from Goat’s Milk Protein and Its Activity Enhancement via Amino Acid Substitution

Foods

... This highlighted that shorter peptide segments were more likely to penetrate the Caco-2 cell membrane. Xue et al. (2023) investigated the transport mechanism of immunoreactive peptides in casein gastrointestinal hydrolysates through Caco-2 monolayer cell membranes. The findings revealed that five immunoreactive peptides could pass through the Caco-2 monolayer cell membrane intact, with longer peptide segments transporting at slower rates. ...

Identification of Immune-Active Peptides in Casein Hydrolysates and Its Transport Mechanism on a Caco-2 Monolayer

Foods