Modification of ACE-inhibitory peptides from Acaudina molpadioidea using the plastein reaction and examination of its mechanism

Jiang, Suisui; Zhao, Yuanhui; Shen, Qingqing; Zhu, Xianjin; Dong, Shiyuan; Liu, Zunying; Wu, Haohao; Zeng, Mingyong

doi:10.1016/j.fbio.2018.08.008

Cited by 9 publications

(8 citation statements)

References 31 publications

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“…As shown in Figure 2A, the hydrophobicity index of the plastein products steadily increased over 3 h, attaining a maximum of 33.9%. Our results are consistent with those of Jiang et al [19], who reported that the internal hydrophobic amino acids were exposed during the plastein reaction, indicating that hydrophobic interactions are important forces in the formation of plastein products. Similarly, the zinc-binding capacity of the plastein products continuously increased for 3 h (Figure 2B).…”

Section: Resultssupporting

confidence: 93%

“…The synthetic reaction dominated the plastein reaction and it inevitably led to a decrease in the free amino acids in the reaction system [17,19]. To improve the efficiency of the plastein reaction, the effects of hydrolysis pH, temperature, substrate concentration, pepsin dosage, reaction time, and glutamate concentration on the decrease in the free amino acid content of the plastein products were optimized in the present study.…”

Section: Resultsmentioning

confidence: 99%

“…The free amino acids were detected based on the O -phthaldialdehyde (OPA) method [19]. Briefly, 100 μL of oyster plastein products was added to 2 mL of OPA reagent (40 mg/mL).…”

Section: Methodsmentioning

confidence: 99%

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Oyster-Derived Zinc-Binding Peptide Modified by Plastein Reaction via Zinc Chelation Promotes the Intestinal Absorption of Zinc

Chen

Wang

et al. 2019

Marine Drugs

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Zinc-binding peptides from oyster (Crassostrea gigas) have potential effects on zinc supplementation. The aim of this study was to prepare efficient zinc-binding peptides from oyster-modified hydrolysates by adding exogenous glutamate according to the plastein reaction and to further explore the zinc absorption mechanism of the peptide-zinc complex (MZ). The optimum conditions for the plastein reaction were as follows: pH 5.0, 40 °C, substrate concentration of 40%, pepsin dosage of 500 U/g, reaction time of 3 h and l-[1-13C]glutamate concentration of 10 mg/mL. The results of 13C isotope labelling suggested that the addition of l-[1-13C]glutamate contributed to the increase in the zinc-binding capacity of the peptide. The hydrophobic interaction was the main mechanism of action of the plastein reaction. Ultraviolet spectra and scanning electronic microscopy (SEM) revealed that the zinc-binding peptide could bind with zinc and form MZ. Furthermore, MZ could significantly enhance zinc bioavailability in the presence of phytic acid, compared to the commonly used ZnSO4. Additionally, MZ significantly promoted the intestinal absorption of zinc mainly through two pathways, the zinc ion channel and the small peptide transport pathway. Our work attempted to increase the understanding of the zinc absorption mechanism of MZ and to support the potential application of MZ as a supplementary medicine.

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Section: Resultssupporting

confidence: 93%

Section: Resultsmentioning

confidence: 99%

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Oyster-Derived Zinc-Binding Peptide Modified by Plastein Reaction via Zinc Chelation Promotes the Intestinal Absorption of Zinc

Chen

Wang

et al. 2019

Marine Drugs

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“…Several bioactive compounds were isolated from A. molpadioides that produced various biological and pharmacological activities such as the use of fucoidan as an agent to reduce side-effects of gastrointestinal mucosits during chemotherapy ( Zuo et al, 2015 ), beneficial effect of cerebroside in ameliorating non-alcoholic fatty liver disease ( Xu et al, 2011 ), inhibition of angiotensin converting enzyme (ACE) for hypertension management ( Zhao et al, 2009 , Jiang et al, 2018 ) and sources of antioxidants ( Bordbar et al, 2011 ). A. molpadioides derived fucosylated chondroitin sulphate was reported to be antiadipogenic by decreasing the expression of SREBP-1c, PPARγ and C/EBP indicating the possibility of interaction with PCSK9 gene ( Xu et al, 2015 ).…”

Section: Discussionmentioning

confidence: 99%

Acaudina molpadioides mediates lipid uptake by suppressing PCSK9 transcription and increasing LDL receptor in human liver cells

Jack

Mohd

Kamaruddin

et al. 2021

Saudi Journal of Biological Sciences

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Acaudina molpadioides has been long used as traditional medicinal resources and reported to demonstrate various important bioactivities such as anticoagulation, antithrombosis, anti-hyperglycemia and anticancer. However, its lipid lowering activity is yet to be fully explored. Proprotein convertase subtilisin/kexin type 9 (PCSK9) is an enzyme that enhances the lysosomal degradation of hepatic low density lipoprotein receptor (LDLR) resulting in excessive accumulation of the plasma levels of LDL-cholesterols (LDL-C) which subsequently accelerate atherosclerosis. In the present study, A. molpadioides fractions were subjected to promoter-reporter luciferase assay to determine its role as PCSK9 inhibitors. It was found both fractions (EFA and EFB) reduced the transcriptional activity of PCSK9 promoter. Among the seven 5′end deletion constructs of PCSK9 promoter, fragments D1 (−1,711/−94), D3 (−709/−94) and D4 (−440/−94), were suppressed in the presence of both fractions whereas D2 (−1,214/−94), and, D6 (−351/−94) as well as D7 (−335/−94) were inhibited only by EFA and EFB, respectively. Further transcription factor binding sites prediction using MatInspector software discovered various potential cis -regulatory elements namely, PPAR, KLFs, RBPJ-kappa and SREBP that may potentially be involved in ameliorating the transcriptional activity of PCSK9. Immunofluorescence staining was used to evaluate the effects of both fractions on LDL-C and LDLR. Results showed that levels of LDL-C uptake in EFA-treated cells were 69.1% followed by EFB at 32.6%, as compared to untreated control after 24 h treatment. The LDLR protein distribution was induced by 62.41% and 32.2%, which corresponded to an increase in LDL-C uptake in both EFA and EFB treatment, respectively. Hence, the inhibition of PCSK9 by bioactive compounds in EFA and EFB could be another promising therapeutic agent in reducing the cholesterol levels and atherosclerosis by targeting PCSK9.

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“…This reaction can also cause bioactivity changes in protein hydrolysates. For example, it was observed that the plastein reaction of the chicken plasma protein and sea cucumber hydrolysates led to improved inhibition of the angiotensin-converting enzyme (ACE) [ 8 , 9 ], and that of soy protein hydrolysates resulted in higher anti-platelet activity [ 10 ]. Moreover, the plastein products enriched with exogenous phenylalanine (Phe) or tyrosine (Tyr) could provide a protective activity in the hepatocytes against the H 2 O 2 - or ethanol-induced damage [ 11 , 12 ].…”

Section: Introductionmentioning

confidence: 99%

Impact of the Plastein Reaction of Casein Hydrolysates in the Presence of Exogenous Amino Acids on Their Anti-Inflammatory Effect in the Lipopolysaccharide-Stimulated Macrophages

Shi

Zhao

2022

Foods

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In this study, papain-generated casein hydrolysates (CH) with a degree of hydrolysis of 13.7% were subjected to a papain-mediated plastein reaction in the absence or presence of one of the exogenous amino acids—Gly, Pro, and Hyp—to prepare four plastein modifiers, or mixed with one of three amino acids to prepare three mixtures. The assay results confirmed that the reaction reduced free NH2 for the modifiers and caused amino acid incorporation and peptide condensation. When RAW264.7 macrophages were exposed to the CH, modifiers, and mixtures, these samples promoted macrophage growth and phagocytosis in a dose-dependent manner. In addition, the CH shared similar activity in the cells as the mixtures, while the modifiers (especially the PCH-Hyp prepared with Hyp addition) exerted higher potential than CH, the mixtures, and PCH (the modifier prepared without amino acid addition). The plastein reaction thus enhanced CH bioactivity in the cells. When RAW264.7 macrophages were stimulated with lipopolysaccharide (LPS), the inflammatory cells produced more lactate dehydrogenase (LDH) release and reactive oxygen species (ROS) formation, and caused more four inflammatory mediators (NO, PGE2, TNF-α, and IL-6) and two anti-inflammatory mediators (TGF-β1 and IL-10). However, the PCH-Hyp, PCH, and CH at dose levels of 100 μg/mL could combat against the LPS-induced inflammation. Overall, the PCH-Hyp was more active than the CH and PCH in reducing LDH release, ROS formation, and the secretion of these inflammatory mediators, or in increasing the secretion of the anti-inflammatory mediators. The qPCR and Western blot analysis results further confirmed that these samples had anti-inflammatory effects on the stimulated cells by suppressing the LPS-induced activation of the NF-κB signaling pathway, via regulating the mRNA/miRNA expression of iNOS, IL-6, TNF-α, IL-1β, COX-2, TLR4, IL-10, TGF-β1, miR-181a, miR-30d, miR-155, and miR-148, as well as the protein expression of MyD88, p-IKKα, p-IκBα, p-NF-κB p65, and iNOS, involved in this signaling pathway. In addition, the immunofluorescence assay results revealed that these samples could block the LPS-mediated nuclear translocation of the p65 protein and displayed the same function as the NF-κB inhibitor BAY 11-7082. It was concluded that CH could be endowed with higher anti-inflammatory activity to the macrophages by performing a plastein reaction, particularly that in the presence of exogenous Hyp.

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Modification of ACE-inhibitory peptides from Acaudina molpadioidea using the plastein reaction and examination of its mechanism

Cited by 9 publications

References 31 publications

Oyster-Derived Zinc-Binding Peptide Modified by Plastein Reaction via Zinc Chelation Promotes the Intestinal Absorption of Zinc

Oyster-Derived Zinc-Binding Peptide Modified by Plastein Reaction via Zinc Chelation Promotes the Intestinal Absorption of Zinc

Acaudina molpadioides mediates lipid uptake by suppressing PCSK9 transcription and increasing LDL receptor in human liver cells

Impact of the Plastein Reaction of Casein Hydrolysates in the Presence of Exogenous Amino Acids on Their Anti-Inflammatory Effect in the Lipopolysaccharide-Stimulated Macrophages

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