Exploration of interaction between porcine myofibrillar proteins and selected ketones by GC–MS, multiple spectroscopy, and molecular docking approaches

Wang, Rui; Zhang, Hongwei; Liu, Qian; Xia, Xiufang; Chen, Qian; Kong, Baohua

doi:10.1016/j.foodres.2022.111624

Cited by 31 publications

(12 citation statements)

References 45 publications

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“…In addition, we found the presence of amino acids (such as Tyr and Phe) capable of inducing intrinsic fluorescence in the active pocket of 2‐pentylfuran bound to proteins, which explained the fluorescence quenching that can be induced by protein adsorption of 2‐pentylfuran. Similar results were reported by Wang 28 . Combining the results of both fluorescence and molecular docking, in the SPI‐flavor and PnPI‐flavor systems, not only are there hydrophobic interactions but also some electrostatic interactions and hydrogen bonding can be observed.…”

Section: Resultssupporting

confidence: 87%

“…Typically, the absorption peak at around 280 nm was contributed by the indazole ring of tryptophan residue and the phenolic group of tyrosine (Tyr) residue, while the phenylalanine (Phe) reacted at 260 nm 27 . Previous studies have shown that aromatic amino acids are closely related to the hydrophobic microenvironment 14,28 . The results revealed that 2‐pentylfuran altered the hydrophobic microenvironment of the three plant proteins in the protein–flavor binding system.…”

Section: Resultsmentioning

confidence: 97%

“…27 Previous studies have shown that aromatic amino acids are closely related to the hydrophobic microenvironment. 14,28 The results revealed that 2-pentylfuran altered the hydrophobic microenvironment of the three plant proteins in the protein-flavor binding system. In general, the UV spectroscopy method allowed a rapid observation of 2-pentylfuran affecting the microenvironment of the three plant proteins, but this was a composite result for rapid screening only.…”

Section: Discussionmentioning

confidence: 99%

“…Similar results were reported by Wang. 28 Combining the results of both fluorescence and molecular docking, in the SPI-flavor and PnPI-flavor systems, not only are there hydrophobic interactions but also some electrostatic interactions and hydrogen bonding can be observed. In addition, it appeared that 2-pentylfuran bound more strongly to SPI than PnPI, although they both relied on hydrophobic interactions, electrostatic interactions and hydrogen bonds.…”

Section: Molecular Docking Analysesmentioning

confidence: 97%

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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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Section: Resultssupporting

confidence: 87%

Section: Resultsmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Section: Molecular Docking Analysesmentioning

confidence: 97%

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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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“…32,33 At 298 K, 303 K and 313 K, the uorescence quenching rate constant k q was much larger than the maximum dynamic quenching constant (2.0 × 10 10 L (mol −1 s −1 )), this result indicates that TA and BSA play an important role in the binding of them in a static quenching mode as a base-state stable complex. 34,35 Therefore, it is suggested that the interaction mode of TA with BSA is static quenching.…”

Section: Analysis Of Uorescence Quenching Typesmentioning

confidence: 99%

Insight into the interaction between tannin acid and bovine serum albumin from a spectroscopic and molecular docking perspective

Ning

Cao

et al. 2023

RSC Adv.

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Rapid screening, isolation, and activity evaluation of potential xanthine oxidase inhibitors in Polyporus umbellatus and mechanism of action in the treatment of gout

Liu,

Zhuang,

et al. 2023

Phytochemical Analysis

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IntroductionStudies show that Polyporus umbellatus has some pharmacological effects in enhancing immunity and against gout.ObjectivesWe aimed to establish new techniques for extraction, biological activity screening, and preparation of xanthine oxidase inhibitors (XODIs) from P. umbellatus.MethodsFirst, the extraction of P. umbellatus was investigated using the back propagation (BP) neural network genetic algorithm mathematical regression model, and the extraction variables were optimised to maximise P. umbellatus yield. Second, XODIs were rapidly screened using ultrafiltration, and the change of XOD activity was tested by enzymatic reaction kinetics experiment to reflect the inhibitory effect of active compounds on XOD. Meanwhile, the potential anti‐gout effects of the obtained active substances were verified using molecular docking, molecular dynamics simulations, and network pharmacology analysis. Finally, with activity screening as guide, a high‐speed countercurrent chromatography (HSCCC) method combined with consecutive injection and two‐phase solvent system preparation using the UNIFAC mathematical model was successfully developed for separation and purification of XODIs, and the XODIs were identified using MS and NMR.ResultsThe results verified that polyporusterone A, polyporusterone B, ergosta‐4,6,8(14),22‐tetraen‐3‐one, and ergosta‐7,22‐dien‐3‐one of P. umbellatus exhibited high biological affinity towards XOD. Their structures have been further identified by NMR, indicating that the method is effective and applicable for rapid screening and identification of XODIs.ConclusionThis study provides new ideas for the search for natural XODIs active ingredients, and the study provide valuable support for the further development of functional foods with potential therapeutic benefits.

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Exploration of interaction between porcine myofibrillar proteins and selected ketones by GC–MS, multiple spectroscopy, and molecular docking approaches

Cited by 31 publications

References 45 publications

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

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

Insight into the interaction between tannin acid and bovine serum albumin from a spectroscopic and molecular docking perspective

Rapid screening, isolation, and activity evaluation of potential xanthine oxidase inhibitors in Polyporus umbellatus and mechanism of action in the treatment of gout

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