Wei Liu , Songming Li , Zhaoxia Cai , Yi Wang , Meiyu Liu , Xi Huang
{"title":"从光维素水解物中鉴定一种新的钙转运促进肽:Caco-2细胞单层的建立、序列测定和分子相互作用分析","authors":"Wei Liu , Songming Li , Zhaoxia Cai , Yi Wang , Meiyu Liu , Xi Huang","doi":"10.1016/j.fbio.2025.106825","DOIUrl":null,"url":null,"abstract":"<div><div>This research aimed to purify and identify calcium transport-promoting peptides from phosvitin hydrolysate (PPPs) using anion-exchange chromatography, Caco-2 cell monolayer assays, determining peptide sequence, and molecular docking. Four fractions were obtained from PPPs using anion-exchange chromatography. The third fraction (PPP3) exhibited the highest calcium chelating capacity (98.10 ± 0.92 %) at a peptide to calcium mass ratio of 6 to 1. Based on the Caco-2 cell monolayers, PPP3 exhibited the highest calcium transport-promoting activity compared to PPPs, which might be associated with the transient receptor potential vanilloid 6 (TRPV6) channel. The sequences of peptides were identified from PPP3 using chromatography-tandem mass spectrometry. Eight peptides with <1 kDa molecular weights and <10 amino acids were docked to TRPV6 protein. Among them, LSKIWGR, a water-soluble peptide, showed the highest binding affinity with TRPV6 through hydrogen bonds and hydrophobic interactions, which was −8.4 kcal/mol. Compared to the PPP3 component, LSKIWGR showed a stronger enhancement of calcium transport (10.55 ± 0.10 μg/well) on the Caco-2 cell monolayer. In summary, this study isolated a novel peptide (LSKIWGR) from PPPs that promotes calcium transport <em>via</em> the TRPV6 channel. It provides a theoretical basis for further investigation of its calcium transport-promoting activity <em>in vivo.</em></div></div>","PeriodicalId":12409,"journal":{"name":"Food Bioscience","volume":"69 ","pages":"Article 106825"},"PeriodicalIF":4.8000,"publicationDate":"2025-05-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Identification of a novel calcium transport-promoting peptide from phosvitin Hydrolysate: Establishment of a Caco-2 cell monolayer, sequence determination, and molecular interaction analysis\",\"authors\":\"Wei Liu , Songming Li , Zhaoxia Cai , Yi Wang , Meiyu Liu , Xi Huang\",\"doi\":\"10.1016/j.fbio.2025.106825\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>This research aimed to purify and identify calcium transport-promoting peptides from phosvitin hydrolysate (PPPs) using anion-exchange chromatography, Caco-2 cell monolayer assays, determining peptide sequence, and molecular docking. Four fractions were obtained from PPPs using anion-exchange chromatography. The third fraction (PPP3) exhibited the highest calcium chelating capacity (98.10 ± 0.92 %) at a peptide to calcium mass ratio of 6 to 1. Based on the Caco-2 cell monolayers, PPP3 exhibited the highest calcium transport-promoting activity compared to PPPs, which might be associated with the transient receptor potential vanilloid 6 (TRPV6) channel. The sequences of peptides were identified from PPP3 using chromatography-tandem mass spectrometry. Eight peptides with <1 kDa molecular weights and <10 amino acids were docked to TRPV6 protein. Among them, LSKIWGR, a water-soluble peptide, showed the highest binding affinity with TRPV6 through hydrogen bonds and hydrophobic interactions, which was −8.4 kcal/mol. Compared to the PPP3 component, LSKIWGR showed a stronger enhancement of calcium transport (10.55 ± 0.10 μg/well) on the Caco-2 cell monolayer. In summary, this study isolated a novel peptide (LSKIWGR) from PPPs that promotes calcium transport <em>via</em> the TRPV6 channel. It provides a theoretical basis for further investigation of its calcium transport-promoting activity <em>in vivo.</em></div></div>\",\"PeriodicalId\":12409,\"journal\":{\"name\":\"Food Bioscience\",\"volume\":\"69 \",\"pages\":\"Article 106825\"},\"PeriodicalIF\":4.8000,\"publicationDate\":\"2025-05-13\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Bioscience\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2212429225010016\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"FOOD SCIENCE & TECHNOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Bioscience","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2212429225010016","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
Identification of a novel calcium transport-promoting peptide from phosvitin Hydrolysate: Establishment of a Caco-2 cell monolayer, sequence determination, and molecular interaction analysis
This research aimed to purify and identify calcium transport-promoting peptides from phosvitin hydrolysate (PPPs) using anion-exchange chromatography, Caco-2 cell monolayer assays, determining peptide sequence, and molecular docking. Four fractions were obtained from PPPs using anion-exchange chromatography. The third fraction (PPP3) exhibited the highest calcium chelating capacity (98.10 ± 0.92 %) at a peptide to calcium mass ratio of 6 to 1. Based on the Caco-2 cell monolayers, PPP3 exhibited the highest calcium transport-promoting activity compared to PPPs, which might be associated with the transient receptor potential vanilloid 6 (TRPV6) channel. The sequences of peptides were identified from PPP3 using chromatography-tandem mass spectrometry. Eight peptides with <1 kDa molecular weights and <10 amino acids were docked to TRPV6 protein. Among them, LSKIWGR, a water-soluble peptide, showed the highest binding affinity with TRPV6 through hydrogen bonds and hydrophobic interactions, which was −8.4 kcal/mol. Compared to the PPP3 component, LSKIWGR showed a stronger enhancement of calcium transport (10.55 ± 0.10 μg/well) on the Caco-2 cell monolayer. In summary, this study isolated a novel peptide (LSKIWGR) from PPPs that promotes calcium transport via the TRPV6 channel. It provides a theoretical basis for further investigation of its calcium transport-promoting activity in vivo.
Food BioscienceBiochemistry, Genetics and Molecular Biology-Biochemistry
CiteScore
6.40
自引率
5.80%
发文量
671
审稿时长
27 days
期刊介绍:
Food Bioscience is a peer-reviewed journal that aims to provide a forum for recent developments in the field of bio-related food research. The journal focuses on both fundamental and applied research worldwide, with special attention to ethnic and cultural aspects of food bioresearch.