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Lunasin-like Peptide in Legume and Cereal Seeds: A Review
Jorge Oswaldo Gutiérrez-López1, Erick Damián Castañeda-Reyes1, Gloria Dávila-Ortiz1
1Protein of Vegetal Origin Laboratory, Biochemistry Engineering Department, Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Av. Wilfrido Massieu s/n, Zacantenco, Gustavo A. Madero, Mexico City 07738, Mexico.
Abstract:
Lunasin is a peptide found in the soybean albumin 2S subunit, which has important bioactivities, such as anticancer and antioxidant. Recently, peptides similar to soybean lunasin have been reported in other cereal and legume seeds; for this reason, it is considered important to carry out a review that compiles this information, whose interest lies mainly in the bioactive properties of these peptides. The peptides reported in the literature contained in barley, wheat, rye, triticale, oat, black nightshade, amaranth, bean, chickpea, grass pea, lentil, and pea are analyzed and described. Isolation methods such as ion exchange chromatography, immunoaffinity column chromatography, Western blot, reversed-phase chromatography coupled to an electrospray ionization source, extraction with water and dialysis, and extraction with PBS, and tests such as internalization, radical scavenging, chelating, cytotoxicity in cancer cell lines essays, and histone acetyltransferase inhibition essays were carried out to identify their anticancer properties. It is worth mentioning that the in silico analyses of proteins in which the lunasin-like peptide is located have been developed in some of these seeds; however, more studies are needed in order to confirm sequence similarity to that of the lunasin peptide. Further work is needed in order to identify the sequence of these lunasin-like peptides and corroborate their similarity to that of the lunasin, such as the development of specific antibodies for each lunasin-like peptide reported in each type of seeds. This document aims to compile the advances in the research on lunasin-like peptides and their bioactivities to have a better understanding of the current advances related to these peptides.
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