Scalable purification and characterization of the anticancer lunasin peptide from soybean.

Lunasin is a peptide derived from the soybean 2S albumin seed protein that has both anticancer and anti-inflammatory activities. Large-scale animal studies and human clinical trials to determine the efficacy of lunasin in vivo have been hampered by the cost of synthetic lunasin and the lack of a met...

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Autores principales:	Lauren E Seber, Brian W Barnett, Elizabeth J McConnell, Steven D Hume, Jian Cai, Kati Boles, Keith R Davis
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/55a0a8fbbf2d4e8d87ec172f64023256
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spelling	oai:doaj.org-article:55a0a8fbbf2d4e8d87ec172f640232562021-11-18T07:22:09ZScalable purification and characterization of the anticancer lunasin peptide from soybean.1932-620310.1371/journal.pone.0035409https://doaj.org/article/55a0a8fbbf2d4e8d87ec172f640232562012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22514740/?tool=EBIhttps://doaj.org/toc/1932-6203Lunasin is a peptide derived from the soybean 2S albumin seed protein that has both anticancer and anti-inflammatory activities. Large-scale animal studies and human clinical trials to determine the efficacy of lunasin in vivo have been hampered by the cost of synthetic lunasin and the lack of a method for obtaining gram quantities of highly purified lunasin from plant sources. The goal of this study was to develop a large-scale method to generate highly purified lunasin from defatted soy flour. A scalable method was developed that utilizes the sequential application of anion-exchange chromatography, ultrafiltration, and reversed-phase chromatography. This method generates lunasin preparations of >99% purity with a yield of 442 mg/kg defatted soy flour. Mass spectrometry of the purified lunasin revealed that the peptide is 44 amino acids in length and represents the original published sequence of lunasin with an additional C-terminal asparagine residue. Histone-binding assays demonstrated that the biological activity of the purified lunasin was similar to that of synthetic lunasin. This study provides a robust method for purifying commercial-scale quantities of biologically-active lunasin and clearly identifies the predominant form of lunasin in soy flour. This method will greatly facilitate the development of lunasin as a potential nutraceutical or therapeutic anticancer agent.Lauren E SeberBrian W BarnettElizabeth J McConnellSteven D HumeJian CaiKati BolesKeith R DavisPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 4, p e35409 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Lauren E Seber Brian W Barnett Elizabeth J McConnell Steven D Hume Jian Cai Kati Boles Keith R Davis Scalable purification and characterization of the anticancer lunasin peptide from soybean.
description	Lunasin is a peptide derived from the soybean 2S albumin seed protein that has both anticancer and anti-inflammatory activities. Large-scale animal studies and human clinical trials to determine the efficacy of lunasin in vivo have been hampered by the cost of synthetic lunasin and the lack of a method for obtaining gram quantities of highly purified lunasin from plant sources. The goal of this study was to develop a large-scale method to generate highly purified lunasin from defatted soy flour. A scalable method was developed that utilizes the sequential application of anion-exchange chromatography, ultrafiltration, and reversed-phase chromatography. This method generates lunasin preparations of >99% purity with a yield of 442 mg/kg defatted soy flour. Mass spectrometry of the purified lunasin revealed that the peptide is 44 amino acids in length and represents the original published sequence of lunasin with an additional C-terminal asparagine residue. Histone-binding assays demonstrated that the biological activity of the purified lunasin was similar to that of synthetic lunasin. This study provides a robust method for purifying commercial-scale quantities of biologically-active lunasin and clearly identifies the predominant form of lunasin in soy flour. This method will greatly facilitate the development of lunasin as a potential nutraceutical or therapeutic anticancer agent.
format	article
author	Lauren E Seber Brian W Barnett Elizabeth J McConnell Steven D Hume Jian Cai Kati Boles Keith R Davis
author_facet	Lauren E Seber Brian W Barnett Elizabeth J McConnell Steven D Hume Jian Cai Kati Boles Keith R Davis
author_sort	Lauren E Seber
title	Scalable purification and characterization of the anticancer lunasin peptide from soybean.
title_short	Scalable purification and characterization of the anticancer lunasin peptide from soybean.
title_full	Scalable purification and characterization of the anticancer lunasin peptide from soybean.
title_fullStr	Scalable purification and characterization of the anticancer lunasin peptide from soybean.
title_full_unstemmed	Scalable purification and characterization of the anticancer lunasin peptide from soybean.
title_sort	scalable purification and characterization of the anticancer lunasin peptide from soybean.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/55a0a8fbbf2d4e8d87ec172f64023256
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Scalable purification and characterization of the anticancer lunasin peptide from soybean.

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