Study on interaction between curcumin and pepsin by spectroscopic and docking methods

Ying, Ming; Huang, Fenglan; Ye, Haidong; Xu, Hong; Shen, Liangliang; Huan, Tianwen; Sheng, Huang; Xie, Jiangfeng; Tian, Sijia; Hu, Zhangli; He, Zhendan; Lu, Jun; Zhou, Kai

doi:10.1016/j.ijbiomac.2015.04.057

Cited by 83 publications

(32 citation statements)

References 33 publications

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“…In other CD studies on small molecule polyphenols and pepsin (Li et al., ; Ying et al., ), the addition of small molecule polyphenols also reduced the amount of β‐sheet, both parallel and antiparallel, in pepsin (EGCG decreased β‐sheet from 35.2% to 30.2%, whereas curcumin reduced it from 54.5% to 45.3%), but this decrease was much higher than the OeB‐mediated decrease in pepsin β‐sheet. Therefore, OeB can have a certain effect on the secondary structure of pepsin, but its effect is less than the effect of small molecule polyphenols on pepsin, which may be due to the weaker hydrophobic interaction between pepsin and OeB.…”

Section: Resultsmentioning

confidence: 77%

“…If it is inhibited, it will lead to a decrease in protein digestibility and a decrease in nutrient titer, causing adverse reactions such as indigestion, loss of appetite, and even growth stagnation. Pepsin is a small (35 kDa) globular protein consisting of 326 amino acid residues (Figure C) with two structurally homologous domains (Ying et al., ). The active binding site of pepsin is located in the cleft between the two domains and is formed from the two aspartate residues Asp32 and Asp215 (Jin et al., ).…”

Section: Introductionmentioning

confidence: 99%

“…The active binding site of pepsin is located in the cleft between the two domains and is formed from the two aspartate residues Asp32 and Asp215 (Jin et al., ). A number of studies have shown some polyphenolic compounds can inhibit pepsin, possibility as a result of direct interactions (Karl, And, & Lynn, ; Koo & Noh, ; Shen et al., ; Ying et al., ; Zhang, Cao, Fei, & Wang, ). However, research on the interactions between polyphenols and pepsin has mainly focused on small molecule polyphenols, while the interactions between oligomer ellagitannins, such as OeB, and pepsin remain largely uncharacterized.…”

Section: Introductionmentioning

confidence: 99%

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Investigation on the Interaction Behavior Between Oenothein B and Pepsin by Isothermal Titration Calorimetry and Spectral Studies

Liu

Wang

Shi

et al. 2019

Journal of Food Science

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Oenothein B (OeB) is a dimeric macrocyclic ellagitannin isolated from Herbs and fruits that have a variety of biological activities. In order to better understand the effect of OeB on the activity of the digestive enzyme pepsin, interactions between OeB and pepsin were investigated in vitro under simulated physiological conditions based on enzyme inhibition studies, fluorescence, isothermal titration calorimetry, CD, and molecular docking. It was found OeB is an effective inhibitor of pepsin, likely acting in a reversible manner through both competitive and noncompetitive inhibition. Fluorescence quenching of pepsin by OeB was a static quenching. CD spectra showed the addition of OeB causes the main chain of pepsin to loosen and expand and the partial β‐sheet structure to be converted to a disordered structure. Isothermal titration calorimetry and docking studies revealed the main binding mechanism of OeB and pepsin was through noncovalent interactions, hydrophobic interactions with OeB and the internal hydrophobic group of pepsin, and then hydrogen bonding between OeB and the Val243 and Asp77 residues of pepsin. Noncovalent bonds between OeB and pepsin change the polarity and structure of enzymes, decreasing enzymatic activity. Compared with small molecular polyphenols, OeB has a weaker hydrophobic interaction with pepsin and less effect on the secondary structure of pepsin. These findings are the first direct elucidation of the interactions between the oligomer ellagitannin OeB and pepsin, further contributing to understanding binding between oligomer ellagitannins and digestive enzymes. Practical Application The results of this study indicate that the interaction between OeB and pepsin has a certain inhibitory effect on pepsin. In order to reduce the impact of OeB on human digestion and its own activities, nano‐encapsulation technology can be used in the future to protect oligomeric ellagitannin such as OeB.

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Section: Resultsmentioning

confidence: 77%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Investigation on the Interaction Behavior Between Oenothein B and Pepsin by Isothermal Titration Calorimetry and Spectral Studies

Liu

Wang

Shi

et al. 2019

Journal of Food Science

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“…79 Pepsin has been shown to form complexes with small molecules, indicated by red shifts in wavelength and changes absorbance intensity in UV-vis spectra. 29, 63, 64 Reductions in absorption intensity indicate that the chromophores, tryptophan and tyrosine, are less exposed to the solvent, thus contributing differently to the adsorption coefficient. 65 The present study suggests that the absorption of pepsin to the AgNPs reduced exposure of these chromophores in such a way that the formation of the pepsin-AgNP complex ultimately influenced the tertiary structure of the protein.…”

Section: Discussionmentioning

confidence: 99%

Protein corona-induced modification of silver nanoparticle aggregation in simulated gastric fluid

Ault

Stark

Axson

et al. 2016

Environ. Sci.: Nano

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Due to their widespread incorporation into a range of biomedical and consumer products, the ingestion of silver nanoparticles (AgNPs) is of considerable concern to human health. However, the extent to which AgNPs will be modified within the gastric compartment of the gastrointestinal tract is still poorly understood. Studies have yet to fully evaluate the extent of physicochemical changes to AgNPs in the presence of biological macromolecules, such as pepsin, the most abundant protein in the stomach, or the influence of AgNPs on protein structure and activity. Herein, AgNPs of two different sizes and surface coatings (20 and 110 nm, citrate or polyvinylpyrrolidone) were added to simulated gastric fluid (SGF) with or without porcine pepsin at three pHs (2.0, 3.5, and 5.0), representing a range of values between preprandial (fasted) and postprandial (fed) conditions. Rapid increases in diameter were observed for all AgNPs, with a greater increase in diameter in the presence of pepsin, indicating that pepsin facilitated AgNPs aggregation. AgNPs interaction with pepsin only minimally reduced the protein’s proteolytic functioning capability, with the greatest inhibitory effect caused by smaller (20 nm) particles of both coatings. No changes in pepsin secondary structural elements were observed for the different AgNPs, even at high particle concentrations. This research highlights the size-dependent kinetics of nanoparticle aggregation or dissolution from interaction with biological elements such as proteins in the gastrointestinal tract. Further, these results demonstrate that, in addition to mass, knowing the chemical form and aggregation state of nanoparticles is critical when evaluating toxicological effects from nanoparticle exposure in the body.

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“…CD spectroscopy is one of the most successful techniques used for the structural characterization of proteins . Herein, the influence of acotiamide hydrochloride on the CD spectra of pepsin is shown in Figure B.…”

Section: Resultsmentioning

confidence: 99%

Probing the Interaction between Acotiamide Hydrochloride and Pepsin by Multispectral Methods, Electrochemical Measurements, and Docking Studies

Wang

et al. 2016

J Biochem & Molecular Tox

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The interaction between acotiamide hydrochloride and pepsin was systematically characterized by fluorescence and electrochemical approaches. Fluorescence lifetime measurements showed that acotiamide hydrochloride quenched the intrinsic fluorescence of pepsin with a new complex formation via static mode, which was reconfirmed by cyclic voltammetry results. Both of the binding number and binding constants were calculated from differential pulse voltammetry analysis and fluorescence spectroscopy. The values obtained from the above two methods displayed a relatively high degree of consistency. Thermodynamic parameters suggested that acotiamide hydrochloride interacted with pepsin spontaneously by hydrogen bonding and van der Waals interactions. These results were consistent with the results obtained from molecular docking analysis. As revealed by synchronous fluorescence, three-dimensional fluorescence, Fourier transform infrared spectrometry, and circular dichroism spectra, acotiamide hydrochloride could affect the microenvironment and slightly change the secondary structure of pepsin. Furthermore, acotiamide hydrochloride can inhibit pepsin activity in vitro, as explained by the molecular docking.

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Study on interaction between curcumin and pepsin by spectroscopic and docking methods

Cited by 83 publications

References 33 publications

Investigation on the Interaction Behavior Between Oenothein B and Pepsin by Isothermal Titration Calorimetry and Spectral Studies

Investigation on the Interaction Behavior Between Oenothein B and Pepsin by Isothermal Titration Calorimetry and Spectral Studies

Protein corona-induced modification of silver nanoparticle aggregation in simulated gastric fluid

Probing the Interaction between Acotiamide Hydrochloride and Pepsin by Multispectral Methods, Electrochemical Measurements, and Docking Studies

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