{"title":"大麻籽蛋白的发酵导致与人类维生素d结合蛋白序列相似的肽的形成","authors":"M. Ruggiero, S. Pacini","doi":"10.15761/mri.1000170","DOIUrl":null,"url":null,"abstract":"In this article, we describe how fermentation of hemp seed proteins leads to formation of peptides that share sequence similarities with human vitamin D-binding protein. We compared the amino acid sequence of edestin, the major hexameric globular protein from hemp protein isolates, with that of human vitamin D-binding protein, and we found significant functional similarities. Among the different peptides formed during the process of fermentation, we identified the peptide VLANAFQ of edestin as a promising candidate showing a high degree of functional similarity as well a common pattern of hydrophobicity with the TPTELAKLVNKRSE peptide that is the active site of human vitamin D-binding protein as far as it immune-stimulating, anti-proliferative and anti-migration properties are concerned.","PeriodicalId":93126,"journal":{"name":"Medical research and innovations","volume":"1 1","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2020-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Fermentation of hemp seed proteins leads to formation of peptides that share sequence similarity with human vitamin D-binding protein\",\"authors\":\"M. Ruggiero, S. Pacini\",\"doi\":\"10.15761/mri.1000170\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"In this article, we describe how fermentation of hemp seed proteins leads to formation of peptides that share sequence similarities with human vitamin D-binding protein. We compared the amino acid sequence of edestin, the major hexameric globular protein from hemp protein isolates, with that of human vitamin D-binding protein, and we found significant functional similarities. Among the different peptides formed during the process of fermentation, we identified the peptide VLANAFQ of edestin as a promising candidate showing a high degree of functional similarity as well a common pattern of hydrophobicity with the TPTELAKLVNKRSE peptide that is the active site of human vitamin D-binding protein as far as it immune-stimulating, anti-proliferative and anti-migration properties are concerned.\",\"PeriodicalId\":93126,\"journal\":{\"name\":\"Medical research and innovations\",\"volume\":\"1 1\",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2020-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Medical research and innovations\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.15761/mri.1000170\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Medical research and innovations","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.15761/mri.1000170","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Fermentation of hemp seed proteins leads to formation of peptides that share sequence similarity with human vitamin D-binding protein
In this article, we describe how fermentation of hemp seed proteins leads to formation of peptides that share sequence similarities with human vitamin D-binding protein. We compared the amino acid sequence of edestin, the major hexameric globular protein from hemp protein isolates, with that of human vitamin D-binding protein, and we found significant functional similarities. Among the different peptides formed during the process of fermentation, we identified the peptide VLANAFQ of edestin as a promising candidate showing a high degree of functional similarity as well a common pattern of hydrophobicity with the TPTELAKLVNKRSE peptide that is the active site of human vitamin D-binding protein as far as it immune-stimulating, anti-proliferative and anti-migration properties are concerned.