Caffeoyl substitution changes the inhibition mode of tartaric acid against α-amylase: Analysis of the enzyme inhibition by four caffeic and tartaric acid derivates

Bai, Fangting; Wang, Yueyi; Zhang, Shanbo; Wang, Yutang; Zhang, Jifan; Cao, Junwei; Sun, Lijun

doi:10.1016/j.lwt.2020.109942

Cited by 15 publications

(8 citation statements)

References 28 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Therefore, the decreased catalytic capacity caused by organic acid addition resulted from the acid-oriented denaturation of the enzyme to a large extent that finally caused the enzyme inactivation at a high inhibitor concentration. This result is different from one previous finding that the four organic acids studied, except for CA, caused the reversible inhibition against α-amylase at the available concentrations (15). That is, the acidic pH of the four organic acids contributed less to α-amylase inhibition.…”

Section: The Relationships Between Organic Acid Ph Values and α-Glucosidase Inhibitioncontrasting

confidence: 99%

“…Caffeic and tartaric acid derivates, including caffeic acid, tartaric acid, caftaric acid (one caffeoyl substituted tartaric acid) and chicoric acid (two caffeoyls substituted tartaric acid) (the molecular structures of four compounds shown in Figure 1A) are the predominant organic/phenolic acids existing in green coffee bean, grape and chicory (13,14). The inhibition of these compounds against α-amylase has been reported and it is found that the caffeoyl moiety is able to enter into and interact with the active site of the enzyme, thus enhancing the competitive inhibition of the organic acids (15). As introduced above, both αamylase and α-glucosidase are key enzymes for starch digestion.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Both Acidic pH Value and Binding Interactions of Tartaric Acid With α-Glucosidase Cause the Enzyme Inhibition: The Mechanism in α-Glucosidase Inhibition of Four Caffeic and Tartaric Acid Derivates

Song

Sun

et al. 2021

Front. Nutr.

Self Cite

View full text Add to dashboard Cite

The inhibition mechanism of four caffeic and tartaric acid derivates, including caffeic acid (CA), tartaric acid (TA), caftaric acid (CFA) and chicoric acid (CHA) against α-glucosidase was characterized by substrate depletion, fluorescence quenching, isothermal titration calorimetry (ITC) and molecular docking. TA and CA were found with the highest and no inhibition effect respectively, and caffeoyl substitution at 2 and/or 3-OH of TA significantly decreased its inhibition. The enzyme inhibition effects of organic acids were not in an inhibitor concentration-dependent mode, and there was a rush increase in inhibition at a respective acidic pH value, especially for CFA and CHA, suggesting the important role of acidic pH in the enzyme inhibition for both compounds. Besides, CA, CFA and CHA were shown with strong quenching effects on α-glucosidase fluorescence because of π-conjugations between aromatic ring of caffeoyl moiety and that of enzyme fluorescent residues. However, no fluorescence quenching effect was observed for TA due to lack of aromatic ring. Additionally, a direct binding interaction behavior was observed for TA with α-glucosidase according to the fitted independent binding model in ITC, but not for CFA and CHA. Therefore, both acidic pH and binding interactions of TA with α-glucosidase resulted in the enzyme inhibition.

show abstract

Section: The Relationships Between Organic Acid Ph Values and α-Glucosidase Inhibitioncontrasting

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Both Acidic pH Value and Binding Interactions of Tartaric Acid With α-Glucosidase Cause the Enzyme Inhibition: The Mechanism in α-Glucosidase Inhibition of Four Caffeic and Tartaric Acid Derivates

Song

Sun

et al. 2021

Front. Nutr.

Self Cite

View full text Add to dashboard Cite

show abstract

“…Meanwhile, nutrients, such as polyphenols with antioxidant effects, are also natural inhibitors of α-amylase and α-glucosidase [ 28 ]. Due to the α-amylase and α-glucosidase that exist in the human digestive play a role in elevating blood glucose, which is a threat to diabetics [ 29 ].…”

Section: Resultsmentioning

confidence: 99%

Research on the Consumption Trend, Nutritional Value, Biological Activity Evaluation, and Sensory Properties of Mini Fruits and Vegetables

Wang

et al. 2021

Foods

View full text Add to dashboard Cite

Mini fruits and vegetables (MFV) are pocket fruits and vegetables whose shape and volume are significantly smaller than those widely sold and well-known normal fruits and vegetables (NFV) on the market. Through the research on the market status and consumption trends of MFV, it was found that MFV have recently become a new market favorite. However, compared with NFV, there was found to be no relevant data on sensory quality, nutritional value, safety, etc. of MFV; this could indicate low consumer awareness of MFV, which in turn affects their planting and sales choices, as well as the market scale remaining small. In this context, six MFV with high degree of marketization were selected and compared with their corresponding NFV to evaluate the nutritional value, biological activity, and sensory properties. The results showed the nutritional value of MFV to be mainly related to their species. The nutritional value of MFV derived from immature, tender vegetables was generally lower than that of mature NFV. For example, the content of zeaxanthin in normal maize was 0.43 mg/kg, which was about 2.87 times that of mini maize (0.15 mg/kg). For newly cultivated mini varieties, their nutritional value often had different trends and rules compared with NFV. The nutritional value obtained by consuming MFV is not equal to that obtained by consuming the corresponding NFV of the same weight.

show abstract

“…SQSRS inhibitory effect was uncompetitive, as indicated by the parallel lines, and this means that the peptide will not compete for the binding site with the natural substrate but will bind to the enzyme-substrate complex and prevent conversion of the substrate to products (8,32). Different inhibition modes have been recorded in literature for peptides and phenolic compounds used as AChE inhibitors (8,9,(33)(34)(35). There is a contrast between the catalytic parameters of AChE inhibition by hemp seed peptides (V max 0.0036 -0.025 mM; K m 0.026 -0.66 mM/min; Ki 0.014 -0.025 mg/ml) as reported by Malomo and Aluko (9) and the kinetic values obtained for peptides in the current study.…”

Section: Kinetics Of Acetylcholinesterase Inhibitionmentioning

confidence: 99%

“…In this model, the K m remains similar while V max decreased in the presence of the peptides (Table 2). Non-competitive inhibition means the peptide binds to a nonactive site in an enzyme-substrate complex or free enzyme to reduce the catalytic activity (31)(32)(33)(34)(35). SQSRS inhibitory effect was uncompetitive, as indicated by the parallel lines, and this means that the peptide will not compete for the binding site with the natural substrate but will bind to the enzyme-substrate complex and prevent conversion of the substrate to products (8,32).…”

Section: Kinetics Of Acetylcholinesterase Inhibitionmentioning

confidence: 99%

In vitro inhibition of acetylcholinesterase activity by yellow field pea (Pisum sativum) protein-derived peptides as revealed by kinetics and molecular docking

et al. 2022

View full text Add to dashboard Cite

Compounds with structural similarities to the neurotransmitter (acetylcholine) are mostly used to inhibit the activity of acetylcholinesterase (AChE) in Alzheimer’s disease (AD) therapy. However, the existing drugs only alleviate symptoms of moderate to mild conditions and come with side effects; hence, the search is still on for potent and safer options. In this study, High performance liquid chromatography (HPLC) fractionations of AChE-inhibitory pea protein hydrolysates obtained from alcalase, flavourzyme and pepsin digestions were carried out followed by sequence identification of the most active fractions using mass spectrometry. Subsequently, 20 novel peptide sequences identified from the active fractions were synthesized and five peptides, QSQS, LQHNA, SQSRS, ETRSQ, PQDER (IC50 = 1.53 – 1.61 μg/mL) were selected and analyzed for ability to change AChE protein conformation (fluorescence emission and circular dichroism), kinetics of enzyme inhibition, and enzyme-ligand binding configurations using molecular docking. The kinetics studies revealed different inhibition modes by the peptides with relatively low (<0.02 mM and <0.1 mM) inhibition constant and Michaelis constant, respectively, while maximum velocity was reduced. Conformational changes were confirmed by losses in fluorescence intensity and reduced α-helix content of AChE after interactions with different peptides. Molecular docking revealed binding of the peptides to both the catalytic anionic site and the peripheral anionic site. The five analyzed peptides all contained glutamine (Q) but sequences with Q in the penultimate N-terminal position (LQHNA, SQSRS, and PQDER) had stronger binding affinity. Results from the different analysis in this study confirm that the peptides obtained from enzymatic digestion of pea protein possess the potential to be used as novel AChE-inhibitory agents in AD management.

show abstract

Caffeoyl substitution changes the inhibition mode of tartaric acid against α-amylase: Analysis of the enzyme inhibition by four caffeic and tartaric acid derivates

Cited by 15 publications

References 28 publications

Both Acidic pH Value and Binding Interactions of Tartaric Acid With α-Glucosidase Cause the Enzyme Inhibition: The Mechanism in α-Glucosidase Inhibition of Four Caffeic and Tartaric Acid Derivates

Both Acidic pH Value and Binding Interactions of Tartaric Acid With α-Glucosidase Cause the Enzyme Inhibition: The Mechanism in α-Glucosidase Inhibition of Four Caffeic and Tartaric Acid Derivates

Research on the Consumption Trend, Nutritional Value, Biological Activity Evaluation, and Sensory Properties of Mini Fruits and Vegetables

In vitro inhibition of acetylcholinesterase activity by yellow field pea (Pisum sativum) protein-derived peptides as revealed by kinetics and molecular docking

Contact Info

Product

Resources

About