Critical issues encountered in the analysis of protein-phenolic binding interactions via fluorescence spectroscopy

Condict, Lloyd; Kasapis, Stefan

doi:10.1016/j.foodhyd.2021.107219

Cited by 36 publications

(8 citation statements)

References 19 publications

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“…When some added substances are close to the Trp residues, the fluorescence of the Trp residues will be quenched and the fluorescence intensity of the protease will decrease. [ 25 ] As shown in the Figure 1, with increase in the CAPE concentration, the fluorescence emission peak intensity of the protease at 345 nm gradually decreases and a red shift appears at the excitation wavelength of 280 nm. The results indicated that CAPE interacts with protease to form the CAPE–protease complex and there is a hydrophilic interaction between CAPE and protease.…”

Section: Resultsmentioning

confidence: 97%

“…The 2,2‐diphenyl‐1‐picrylhydrazyl (DPPH) radical scavenging ability was evaluated according to the research method of the previous work with some modification. [ 25 ] An aliquot solution of the Try–CAPE, Pep–CAPE or α ‐Chy‐CAPE solution complexes with the concentrations of 0, 5, 10, 20, 40, or 60 μmol·kg −1 was added to 1 ml DPPH (0.5 mmol·kg −1 in ethanol). The solution was thoroughly mixed and stored at room temperature in the dark for 30 min.…”

Section: Methodsmentioning

confidence: 99%

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Interaction between caffeic acid phenethyl ester and protease: monitoring by spectroscopic and molecular docking approaches

et al. 2022

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The interaction of one anticancer drug (caffeic acid phenethyl ester; CAPE) with three proteases (trypsin, pepsin and α-chymotrypsin) has been investigated with multispectral methods and molecular docking. As an active components in propolis, the findings are of great benefit to metabolism, design, and structural modification of drugs. The results show that CAPE has an obvious ability to quench the trypsin, pepsin, or α-chymotrypsin fluorescence mainly through a static quenching procedure.Trypsin has the largest binding affinity to CAPE, and α-chymotrypsin has the smallest binding affinity to CAPE. The data obtained from thermodynamic parameters and molecular docking prove that the spontaneously interaction between CAPE and each protease is mainly due to a combination of van der Waals (vdW) force and hydrogen bond (H-bond), controlled by an enthalpy-driven process. The binding force, strength, position, and the number of H-bond are further obtained from the results of molecular docking. Through ultraviolet spectroscopy, dynamic light scattering and circular dichroism experiments, the change in the protease secondary structure induced by CAPE was observed. Additionally, the addition of protease had a positive effect on the antioxidative activity of CAPE, and α-chymotrypsin has the greatest effect on the removal of 2,2-diphenyl-1-picrylhydrazyl free radicals by CAPE.α-chymotrypsin, caffeic acid phenethyl ester (CAPE), pepsin, trypsin | INTRODUCTIONCaffeic acid phenethyl ester (CAPE) has been widely used in various regions as a traditional natural medicine. [1] As the main active ingredient of propolis, CAPE has various biological activities, including anticancer, anti-inflammatory, antibacterial, neuroprotective, etc. [2][3][4] In addition, it has a very strong antioxidant capacity, [5] as a polyphenol containing hydroxyl groups in benzenediol. [6] In previous works, the study of the interaction between CAPE and macromolecules mainly focus on the binding mechanism, influencing factors, drug activities, and pharmacology; many theoretical researches have been done.Studies have shown that poly(3-hydroxybutyrate) (PHB) fibre can enhance the antioxidant and antibacterial activities of CAPE. [7] CAPE can inhibit iNOS gene transcription by inhibiting the nuclear factor NF-κB site, and can inhibit the catalytic activity of iNOS, [8] which provides a research basis for the anti-inflammatory and antitumour effects of CAPE. According to reports, after CAPE is compounded with γ-cyclodextrin (γ-CD), the anticancer activity of CAPE will increase. [9] In addition, in the work of this research group, the binding constant of CAPE and bovine serum albumin was $10 6 , of which the main forces are H-bond and vdW force, and the driving mode is enthalpy drive. However, there are few studies on the interaction

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Section: Resultsmentioning

confidence: 97%

Section: Methodsmentioning

confidence: 99%

Interaction between caffeic acid phenethyl ester and protease: monitoring by spectroscopic and molecular docking approaches

et al. 2022

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“…SPI attained the largest K sv value, inferring that 2‐pentylfuran may cause a stronger quenching of SPI intrinsic fluorescence than PnPI and WPI. Therefore, a modified Stern–Volmer equation was applied to determine the binding constant:

\log \frac{(F_{0} - F)}{F} goodbreak= \log K goodbreak+ n_{H} \log ([], Q)

where K is the binding constant and n H is the Hill coefficient (an indicator of binding site cooperativity) 37 . Commonly, the modified model is applied to static quenching originating from the formation of the protein–flavor complex.…”

Section: Resultsmentioning

confidence: 99%

“…where K is the binding constant and n H is the Hill coefficient (an indicator of binding site cooperativity). 37 Commonly, the modified model is applied to static quenching originating from the formation of the protein-flavor complex. High concentrations of 2-pentylfuran were able to induce its dynamic quenching to WPI, so binding constants were calculated by its low concentration data, as was the Hill coefficient (Fig.…”

Section: Fluorescence Quenching Analysismentioning

confidence: 99%

Exploration of molecular interaction between different plant proteins and 2‐pentylfuran: based on multiple spectroscopy and molecular docking

et al. 2023

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BACKGROUND Soy protein, peanut protein and wheat protein are commonly applied in plant‐based products, but specific off‐odor makes it difficult for consumers to accept, with 2‐pentylfuran being one of the most representative flavors. In this study, 2‐pentylfuran was employed as an example to explore the behavior and mechanism of the three proteins in absorbing off‐odors. RESULTS Gas chromatographic–mass spectrometric analysis indicated that different plant proteins were able to adsorb 2‐pentylfuran. Circular dichroism proved 2‐pentylfuran could drive the α‐helix to β‐sheet transition of soy protein, which was not obvious in peanut protein or wheat protein. Ultraviolet spectroscopy tentatively determined that 2‐pentylfuran caused changes in the tyrosine and tryptophan microenvironments of different plant proteins, which were further evidenced by synchronous fluorescence at fixed wavelength intervals of 15 nm and 60 nm. Static quenching of protein intrinsic fluorescence indicated that they formed a stable complex with 2‐pentylfuran, except for wheat protein (dynamic quenching). CONCLUSION The various conformations of the three proteins are the main reason for the difference in flavor retention of protein. Soy protein, peanut protein and wheat protein adsorbing 2‐pentylfuran relies on non‐covalent forces, especially hydrophobic interactions, maintained between the protein and 2‐pentylfuran. © 2023 Society of Chemical Industry.

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“…Proteins or hydrolysates have intrinsic emission fluorescence because of their tryptophan, tyrosine, and phenylalanine residues (Condict & Kasapis, 2022). The fluorescence emission spectra of Try‐pcRHs and Try‐pcRH‐Iron were shown in Figure 4a.…”

Section: Resultsmentioning

confidence: 99%

Iron‐chelating activity of large yellow croaker ( Pseudosciaena crocea ) roe hydrolysates

Hong

et al. 2022

Food Processing Preservation

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In this study, hydrolysates of large yellow croaker (Pseudosciaena crocea) roe were prepared by trypsin (Try‐pcRHs) and papain (Pap‐pcRHs). The degree of hydrolysis (DH), molecular weight distribution and iron chelating capacity of hydrolysates were investigated. Moreover, the chelation mechanism of iron‐hydrolysates complex also was investigated by amino acid composition analysis, fourier transform infrared spectrophotometer, fluorescence spectrophotometer and ultraviolet–visible spectroscopy. These results showed that Try‐pcRHs exhibited higher iron chelating ability with the EC50 value of 0.14 mg/ml than Pap‐pcRHs, which may be due to the higher DH and content of peptide <1 KDa. Furthermore, the Asp, Glu, Ser, Pro, Ile, Phe and His in Try‐pcRHs might contribute to the chelation reaction, and the groups of ‐COOH, C=O, N‐H and C‐O were involved in chealtiong of Try‐pcRHs with iron. Therefore, Try‐pcRHs have the potential to be used as iron supplements in food industries. Practical Applications Large yellow croaker (Pseudosciaena crocea) roes are the main by‐products in the large yellow croaker processing. Previous studies have found that protein isolates from P. crocea roes composed of vitellogenin B, vitellogenin C and vitellogenin contain a large number of serine residues. In this study, we prepared hydrolysates from large yellow croaker roes, and the results showed that trypsin‐hydrolyzed large yellow croaker roes exhibited great iron‐chelating ability and has the potential to be used as a safe and healthy iron supplements in the food industry.

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Critical issues encountered in the analysis of protein-phenolic binding interactions via fluorescence spectroscopy

Cited by 36 publications

References 19 publications

Interaction between caffeic acid phenethyl ester and protease: monitoring by spectroscopic and molecular docking approaches

Interaction between caffeic acid phenethyl ester and protease: monitoring by spectroscopic and molecular docking approaches

Exploration of molecular interaction between different plant proteins and 2‐pentylfuran: based on multiple spectroscopy and molecular docking

Iron‐chelating activity of large yellow croaker ( Pseudosciaena crocea ) roe hydrolysates

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