Cargando…

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

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Soares, Rosana Aparecida Manólio, Mendonça, Simone, de Castro, Luíla Ívini Andrade, Menezes, Amanda Caroline Cardoso Corrêa Carlos, Arêas, José Alfredo Gomes
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4346949/
https://www.ncbi.nlm.nih.gov/pubmed/25690031
http://dx.doi.org/10.3390/ijms16024150
_version_ 1782359767674519552
author Soares, Rosana Aparecida Manólio
Mendonça, Simone
de Castro, Luíla Ívini Andrade
Menezes, Amanda Caroline Cardoso Corrêa Carlos
Arêas, José Alfredo Gomes
author_facet Soares, Rosana Aparecida Manólio
Mendonça, Simone
de Castro, Luíla Ívini Andrade
Menezes, Amanda Caroline Cardoso Corrêa Carlos
Arêas, José Alfredo Gomes
author_sort Soares, Rosana Aparecida Manólio
collection PubMed
description 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.
format Online
Article
Text
id pubmed-4346949
institution National Center for Biotechnology Information
language English
publishDate 2015
publisher MDPI
record_format MEDLINE/PubMed
spelling pubmed-43469492015-04-03 Major Peptides from Amaranth (Amaranthus cruentus) Protein Inhibit HMG-CoA Reductase Activity Soares, Rosana Aparecida Manólio Mendonça, Simone de Castro, Luíla Ívini Andrade Menezes, Amanda Caroline Cardoso Corrêa Carlos Arêas, José Alfredo Gomes Int J Mol Sci Article 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. MDPI 2015-02-16 /pmc/articles/PMC4346949/ /pubmed/25690031 http://dx.doi.org/10.3390/ijms16024150 Text en © 2015 by the authors; licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Soares, Rosana Aparecida Manólio
Mendonça, Simone
de Castro, Luíla Ívini Andrade
Menezes, Amanda Caroline Cardoso Corrêa Carlos
Arêas, José Alfredo Gomes
Major Peptides from Amaranth (Amaranthus cruentus) Protein Inhibit HMG-CoA Reductase Activity
title Major Peptides from Amaranth (Amaranthus cruentus) Protein Inhibit HMG-CoA Reductase Activity
title_full Major Peptides from Amaranth (Amaranthus cruentus) Protein Inhibit HMG-CoA Reductase Activity
title_fullStr Major Peptides from Amaranth (Amaranthus cruentus) Protein Inhibit HMG-CoA Reductase Activity
title_full_unstemmed Major Peptides from Amaranth (Amaranthus cruentus) Protein Inhibit HMG-CoA Reductase Activity
title_short Major Peptides from Amaranth (Amaranthus cruentus) Protein Inhibit HMG-CoA Reductase Activity
title_sort major peptides from amaranth (amaranthus cruentus) protein inhibit hmg-coa reductase activity
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4346949/
https://www.ncbi.nlm.nih.gov/pubmed/25690031
http://dx.doi.org/10.3390/ijms16024150
work_keys_str_mv AT soaresrosanaaparecidamanolio majorpeptidesfromamaranthamaranthuscruentusproteininhibithmgcoareductaseactivity
AT mendoncasimone majorpeptidesfromamaranthamaranthuscruentusproteininhibithmgcoareductaseactivity
AT decastroluilaiviniandrade majorpeptidesfromamaranthamaranthuscruentusproteininhibithmgcoareductaseactivity
AT menezesamandacarolinecardosocorreacarlos majorpeptidesfromamaranthamaranthuscruentusproteininhibithmgcoareductaseactivity
AT areasjosealfredogomes majorpeptidesfromamaranthamaranthuscruentusproteininhibithmgcoareductaseactivity