Antiobesogenic effect of hydrolysates and peptide fractions of porcine collagen after in vitro gastrointestinal digestion

IF 3.1 2区生物学 Q2 BIOCHEMICAL RESEARCH METHODS

Journal of proteomics Pub Date : 2026-01-06 Epub Date: 2025-10-08 DOI:10.1016/j.jprot.2025.105539

Julio A. González-Noriega , Martín Valenzuela-Melendres , Adrián Hernández-Mendoza , Humberto Astiazarán-García , Thalia Islava-Lagarda , Orlando Tortoledo-Ortiz , Ana L. De La Garza-Hernández , Samaria L. Gutierrez-Pacheco , Andrés Alvarez-Armenta , Emmanuel Ríos-Castro , José A. Huerta-Ocampo , E. Aída Peña-Ramos

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Abstract

The present study evaluated the angiotensin-converting enzyme inhibitory activity (ACEi) of a porcine skin collagen hydrolysate (PSCH) and its peptide fractions before and after a simulation of gastrointestinal digestion and their ability to reduce lipid accumulation in adipocytes (LAA). Before digestion, peptide fractions <1 kDa (PF4) had the highest (p < 0.05) ACEia (85.45 %), followed by PSCH (53.54 %). Post-digestion, PF4 (IC₅₀: 124.49 μg/mL) decreased its activity; thus, DPF4 (digested PF4) had an ACE IC₅₀ of 204.56 μg/mL, while fraction <1 kDa from digested hydrolysate (FDH) showed the lowest activity (IC₅₀: 313.81 μg/mL). Peptides were identified by LC-MS/MS and homology database search and aligned to peptides widely recognized as ACE inhibitors. Nine peptides were identified as potential ACE inhibitors through docking with the active site cavity of this enzyme (mainly GAXGPXGPQ and GPPGPA), and interaction with Zn (II). Subsequently, adding 600 μg/mL of FDH in preadipocytes reduced 71 % LAA, while DPF4 was less effective (45.5 % reduction). The addition of digested peptide fractions into differentiated adipocytes had a similar (p > 0.05) reduction of LAA of 22–39 %. Therefore, regardless of their differences as ACE inhibitors, digested FDH and DPF4 have a similar potential as anti-obesogenic adjuvants.

Significance

In this study, we evaluated the angiotensin-converting enzyme inhibitory activity of a porcine skin collagen hydrolysate and its peptide fractions before and after a simulation of gastrointestinal digestion and their ability to reduce lipid accumulation in adipocytes. Peptides were identified by LC-MS/MS and homology database search and aligned to peptides widely recognized as ACE inhibitors. Nine peptides were identified as potential ACE inhibitors through docking with the active site cavity of this enzyme (mainly GAXGPXGPQ and GPPGPA), and interaction with Zn (II). Subsequently, adding digested peptide fractions into differentiated adipocytes resulted in a reduction of lipid accumulation in adipocytes.

Abstract Image

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猪胶原蛋白水解物和肽段体外胃肠道消化后的抗肥胖作用。

本研究评估了猪皮肤胶原水解物（PSCH）及其肽组分在模拟胃肠道消化前后的血管紧张素转换酶抑制活性（ACEi）以及它们减少脂肪细胞（LAA）中脂质积累的能力。消化前肽段50:124.49 μg/mL)使其活性降低；因此，DPF4（消化的PF4）的ACE IC50为204.56 μg/mL，而分数为50:313.81 μg/mL)。通过LC-MS/MS和同源数据库检索鉴定了肽段，并与广泛认为是ACE抑制剂的肽段进行了比对。通过与ACE酶活性位点空腔对接（主要为GAXGPXGPQ和GPPGPA）以及与Zn （II）相互作用，确定了9个肽段为潜在的ACE抑制剂。随后，在前脂肪细胞中添加600 μg/mL的FDH可使LAA降低71 %，而DPF4的效果较差（降低45.5% %）。在已分化的脂肪细胞中加入消化的肽片段，LAA也有相似的降低（p > 0.05），降低了22-39 %。因此，尽管作为ACE抑制剂存在差异，但消化FDH和DPF4作为抗肥胖佐剂具有相似的潜力。意义：在这项研究中，我们评估了猪皮肤胶原蛋白水解物及其肽组分在模拟胃肠道消化前后的血管紧张素转换酶抑制活性，以及它们减少脂肪细胞中脂质积累的能力。通过LC-MS/MS和同源数据库检索鉴定了肽段，并与广泛认为是ACE抑制剂的肽段进行了比对。通过与ACE酶活性位点空腔对接（主要为GAXGPXGPQ和GPPGPA）以及与Zn （II）相互作用，确定了9个肽段为潜在的ACE抑制剂。随后，将消化的肽组分加入分化的脂肪细胞中，导致脂肪细胞中脂质积累的减少。

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来源期刊

Journal of proteomics 生物-生化研究方法

CiteScore

7.10

自引率

3.00%

发文量

227

审稿时长

73 days

期刊介绍： Journal of Proteomics is aimed at protein scientists and analytical chemists in the field of proteomics, biomarker discovery, protein analytics, plant proteomics, microbial and animal proteomics, human studies, tissue imaging by mass spectrometry, non-conventional and non-model organism proteomics, and protein bioinformatics. The journal welcomes papers in new and upcoming areas such as metabolomics, genomics, systems biology, toxicogenomics, pharmacoproteomics. Journal of Proteomics unifies both fundamental scientists and clinicians, and includes translational research. Suggestions for reviews, webinars and thematic issues are welcome.