Design of a highly potent inhibitory peptide acting as a competitive inhibitor of HMG-CoA reductase

Pak, Valeriy V.; Koo, Minseon; Kwon, Dae Young; Yun, L. M.

doi:10.1007/s00726-012-1276-0

Cited by 45 publications

(35 citation statements)

References 20 publications

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“…1). The calculated IC50 values (222 ± 90, 274 ± 95, and 300 ± 150 µM, respectively, for IAVPGEVA, IAVPTGVA and LPYP) are in reasonable agreement with published results (201, 152, and 484 µM, respectively) (Pak et al, 2005(Pak et al, , 2012.…”

Section: Discussionsupporting

confidence: 88%

“…Pak and co-workers have suggested some parallelism between the mechanism of action of these peptides and statins (Pak et al, 2012). In order to verify whether soy peptides and lovastatin share some intracellular molecular mechanism, HepG2 cells were treated also with lovastatin in similar conditions and immunoblotting and LDL-uptake experiments were performed.…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, the alignment of IAVPGEVA with the glycinin sequence permitted identification of another inhibitory peptide, IAVPTGVA (Pak et al, 2005). Kinetic experiments showed that all these peptides act as competitive inhibitors of HMGCoAR (Pak, Koo, Kwon, & Yun, 2012). These authors, however, used them as leads for the preparation of synthetic analogues, without investigating in detail their mechanism of action in cell cultures.…”

Section: Introductionmentioning

confidence: 94%

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IAVPGEVA, IAVPTGVA, and LPYP, three peptides from soy glycinin, modulate cholesterol metabolism in HepG2 cells through the activation of the LDLR-SREBP2 pathway

Lammi

Zanoni

Arnoldi

2015

Journal of Functional Foods

117

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Section: Discussionsupporting

confidence: 88%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 94%

See 1 more Smart Citation

IAVPGEVA, IAVPTGVA, and LPYP, three peptides from soy glycinin, modulate cholesterol metabolism in HepG2 cells through the activation of the LDLR-SREBP2 pathway

Lammi

Zanoni

Arnoldi

2015

Journal of Functional Foods

117

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“…DVDPR and DPR were reported as inhibitors of lipid absorption. [26] IIAEK was described as reducing the micellar solution of cholesterol in the gut [27]. …”

Section: Resultsmentioning

confidence: 99%

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

Soares

Mendonça

Castro

et al. 2015

IJMS

113

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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.

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“…Tachibana et al attributed that the hypolipidemic effect to the amino acid composition and sequence of the protein isolate, consistent with previous studies of legumes (Moriyama et al, 2004;Lovati et al, 2008). Inhibitory effects of natural (Pak et al, 2005: Soares et al, 2015 and synthetic (Lin et al, 2015;Pak et al, 2008aPak et al, , 2008bPak et al, , 2012 peptides on HMG-CoAr have been reported, but the underlying mechanism remained unclear. Marques et al (2015) and Lammi et al (2015) suggested that legume peptide inhibit HMG-CoAr via the interaction of these peptides with either the active site or NADH-binding site of the enzyme, thus preventing substrate binding to the enzyme and promoting endogenous cholesterol synthesis.…”

Section: Resultsmentioning

confidence: 99%

The Vicilin protein (Vigna radiata L.) of mung bean as a functional food

Amaral

Ferreira

Silva

et al. 2017

NFS

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Purpose-The hypocholesterolemic activity of legume vicilins and the structural homology among mung bean, soybean and adzuki bean vicilins (8S) suggest that this protein may play a role in lipid metabolism. Thus, in the present study, the authors aim to isolate the mung bean vicilin and assess its in vitro effect on 3-hydroxy-3methyl-glutaryl-CoA reductase (HMG CoAr), the enzyme responsible for endogenous cholesterol synthesis. Design/methodology/approach-Chromatographic and electrophoretic characterization identified the molecular mass and polypeptide composition of mung bean vicilin. The hydrolysate of this globulin was obtained by sequential hydrolysis with pepsin-pancreatin and the fragments were characterized by molecular filtration, SDS PAGE and HPLC. Findings-The molecular mass of vicilin was estimated as 158.

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Design of a highly potent inhibitory peptide acting as a competitive inhibitor of HMG-CoA reductase

Cited by 45 publications

References 20 publications

IAVPGEVA, IAVPTGVA, and LPYP, three peptides from soy glycinin, modulate cholesterol metabolism in HepG2 cells through the activation of the LDLR-SREBP2 pathway

IAVPGEVA, IAVPTGVA, and LPYP, three peptides from soy glycinin, modulate cholesterol metabolism in HepG2 cells through the activation of the LDLR-SREBP2 pathway

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

The Vicilin protein (Vigna radiata L.) of mung bean as a functional food

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