Two peptides from soybean β-conglycinin, i.e., YVVNPDNDEN (peptide 2) and YVVNPDNNEN (peptide 3), are known to be absorbed by human enterocytes. The former is a fragment of LRVPAGTTFYVVNPDNDENLRMIA (peptide 1), previously shown to increase the low-density lipoprotein (LDL) uptake and degradation in hepatocytes. Research carried out in silico on their interactions with the catalytic site of 3-hydroxy-3-methylglutaryl CoA reductase (HMGCoAR) demonstrated that they behave as competitive inhibitors of HMGCoAR activity with a statin-like mechanism, confirmed by direct inhibition experiments. Research in HepG2 cells aimed at investigating the effects of these peptides on cholesterol metabolism showed that compared to mock treatment peptide 2 at 350 μM up-regulates the mature SREBP2 protein level by 134.0 ± 10.5%, increases the LDLR protein level by 152.0 ± 20.0%, and enhances the HMGCoAR protein production by 171 ± 29.9%, whereas peptide 3 up-regulates the mature SREBP2 protein level by 158.0 ± 9.2%, increases the LDL level 164.0 ± 17.9%, and induces a HMGCoAR protein increase by 170 ± 50.0%.
Two peptides from soy β-conglycinin induce a hypocholesterolemic effect in hepG2 cells by a statin-like mechanism: comparative in vitro and in silico modeling studies / C. Lammi, C. Zanoni, A. Arnoldi, G. Vistoli. - In: JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY. - ISSN 0021-8561. - 63:36(2015 Aug 27), pp. 7945-7951.
Two peptides from soy β-conglycinin induce a hypocholesterolemic effect in hepG2 cells by a statin-like mechanism: comparative in vitro and in silico modeling studies
C. LammiPrimo
;C. ZanoniSecondo
;A. Arnoldi
;G. VistoliUltimo
2015
Abstract
Two peptides from soybean β-conglycinin, i.e., YVVNPDNDEN (peptide 2) and YVVNPDNNEN (peptide 3), are known to be absorbed by human enterocytes. The former is a fragment of LRVPAGTTFYVVNPDNDENLRMIA (peptide 1), previously shown to increase the low-density lipoprotein (LDL) uptake and degradation in hepatocytes. Research carried out in silico on their interactions with the catalytic site of 3-hydroxy-3-methylglutaryl CoA reductase (HMGCoAR) demonstrated that they behave as competitive inhibitors of HMGCoAR activity with a statin-like mechanism, confirmed by direct inhibition experiments. Research in HepG2 cells aimed at investigating the effects of these peptides on cholesterol metabolism showed that compared to mock treatment peptide 2 at 350 μM up-regulates the mature SREBP2 protein level by 134.0 ± 10.5%, increases the LDLR protein level by 152.0 ± 20.0%, and enhances the HMGCoAR protein production by 171 ± 29.9%, whereas peptide 3 up-regulates the mature SREBP2 protein level by 158.0 ± 9.2%, increases the LDL level 164.0 ± 17.9%, and induces a HMGCoAR protein increase by 170 ± 50.0%.File | Dimensione | Formato | |
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