Major Peptides from Amaranth (Amaranthus cruentus) Protein Inhibit HMG-CoA Reductase Activity

International Journal of Molecular Sciences

Rosana Aparecida Manólio Soares¹  Simone Mendon๺²  Luíla Ívini Andrade de Castro¹  Amanda Caroline Cardoso Corrສ Carlos Menezes¹ 

[1] Faculty of Public Health, University of São Paulo, Av. Dr. Arnaldo, 715, São Paulo 01246-904, SP, Brazil; E-Mails:;EMBRAPA (Brazilian Corporation of Agricultural Research), PqEB, Brasília 70770-200, DF, Brazil; E-Mail:

关键词: bioactive peptides;    de novo sequencing;    mass spectrometry;    amaranth;    HMG-CoA reductase activity;   

DOI  :  10.3390/ijms16024150

来源: mdpi

【 摘 要 】

The objective of this study was to identify the major peptides generated by the in vitro hydrolysis of Amaranthus cruentus protein and to verify the effect of these peptides on the activity of 3-hydroxy-3-methyl-glutaryl-CoA reductase (HMG-CoA reductase), a key enzyme in cholesterol biosynthesis. A protein isolate was prepared, and an enzymatic hydrolysis that simulated the in vivo digestion of the protein was performed. After hydrolysis, the peptide mixture was filtered through a 3 kDa membrane. The peptide profile of this mixture was determined by reversed phase high performance chromatography (RP-HPLC), and the peptide identification was performed by LC-ESI MS/MS. Three major peptides under 3 kDa were detected, corresponding to more than 90% of the peptides of similar size produced by enzymatic hydrolysis. The sequences identified were GGV, IVG or LVG and VGVI or VGVL. These peptides had not yet been described for amaranth protein nor are they present in known sequences of amaranth grain protein, except LVG, which can be found in amaranth α‑amylase. Their ability to inhibit the activity of HMG-CoA reductase was determined, and we found that the sequences GGV, IVG, and VGVL, significantly inhibited this enzyme, suggesting a possible hypocholesterolemic effect.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.