Interaction mechanisms and structure-affinity relationships between hyperoside and soybean β-conglycinin and glycinin

Wu, Di; Tang, Lan; Duan, Ran; Hu, Xia; Geng, Fang; Zhang, Yin; Peng, Lianxin; Li, Hui

doi:10.1016/j.foodchem.2021.129052

Cited by 63 publications

(21 citation statements)

References 38 publications

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“…The following equation was used to calculate the binding constant K, as well as the number of binding sites (n) between BSA and ZnO NRs (Figure 12b) [ 51,52 ] :

\ln [\frac{I_{0} - I}{I}] = \ln [K] + n \ln [C_{ZnO}]

The calculated values of binding sites (n) and binding constant (K) were found to be 1.25 and 0.01267, respectively. This K value may change under different experimental conditions such as in vivo conditions.…”

Section: Resultsmentioning

confidence: 99%

“…The change in the binding constant in vivo may be due to different factors. [ 52–54 ] During the binding process, energy transfer occurs. Energy transfer efficiency (Q eff ) can be expressed by the equation [ 55 ] : Q eff = 1 − (I/I 0 ).…”

Section: Resultsmentioning

confidence: 99%

“…The following equation was used to calculate the binding constant K, as well as the number of binding sites (n) between BSA and ZnO NRs (Figure 12b) [51,52] :…”

Section: Fluorescence Study Of the Bsa-zno Nrs Bioconjugatementioning

confidence: 99%

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Exciton–tryptophan coupling pulse behaviour along with corona formation, binding analysis, and interaction study of ZnO nanorod–serum albumin protein bioconjugate

Bhunia¹,

Jha

Saha

2022

Luminescence

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The bioconjugate of bovine serum albumin (BSA) and zinc oxide nanorods (ZnO NRs) is investigated to explore the behaviour of the tryptophan (Trp)-exciton coupling and corona formation. The pulse like nature of the coupled system between Trp of BSA and exciton of ZnO NRs has been observed after analysis of the optical parameters such as refractive index, susceptibility, and optical dielectric constant. The time constant for tryptophan, exciton surface binding (t 1 ) and reorganization (t 2 ) are found to be (t 1 ) 8 min, 7 min and (t 2 ) 150 min, 114.5 min, respectively. The close proximity binding of BSA with ZnO NRs via tryptophan as well as exciton is responsible for bioconjugate formation. The aggregated structure of BSA is observed from smallangle X-ray scattering study in interaction with ZnO NRs. The change in secondary structure and tertiary deformation of the serum protein have been studied from Fourier transform infrared and emission quenching analyses. The number of binding sites (n) signified to the enhancement of the cooperative binding. The binding has been found to be endothermic and favoured using unfavourable positive enthalpy with a favourable entropy change from the result of the isothermal titration calorimetry.

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“…The following equation was used to calculate the binding constant K, as well as the number of binding sites (n) between BSA and ZnO NRs (Figure 12b) [ 51,52 ] :

\ln [\frac{I_{0} - I}{I}] = \ln [K] + n \ln [C_{ZnO}]

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Exciton–tryptophan coupling pulse behaviour along with corona formation, binding analysis, and interaction study of ZnO nanorod–serum albumin protein bioconjugate

Bhunia¹,

Jha

Saha

2022

Luminescence

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“…By plotting log [( F0 – F )/ F ] against log [VD 3 ], a linear curve is obtained with a slope of n . The intercept provides the value of log Ka ( Wu et al, 2020 , 2021 ).…”

Section: Methodsmentioning

confidence: 99%

Ultrasound-assisted pH-shifting remodels egg-yolk low-density lipoprotein to enable construction of a stable aqueous solution of vitamin D3

Wang²,

Wang³

et al. 2022

Current Research in Food Science

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“…[2] Vine tea (or Mao Yan Mei) and MY or DMY have antioxidant, anti-inflammatory, lipid-lowering, hepatoprotective, antibacterial, and protects vision pharmacological activities. [3][4][5][6][7][8][9][10][11][12][13][14][15][16] The interaction between small molecules and protein is helpful to understand the pharmacokinetic behavior of small molecule. Since the MY and DMY are abundant in food and daily intake of them by human is considerable, studying the interaction between MY or DMY and protease is essential.…”

mentioning

confidence: 99%

Investigation on the interaction between myricetin and dihydromyricetin with trypsin, α‐chymotrypsin, lysozyme by spectroscopy and molecular docking methods

Meng

Nan

Shi³

et al. 2022

Luminescence

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The interaction between myricetin and dihydromyricetin with trypsin, α-chymotrypsin and lysozyme was investigated using multispectral and molecular docking methods. The results of fluorescence quenching revealed that myricetin and dihydromyricetin could quench the intrinsic fluorescence of three different proteinases through a static quenching procedure. The binding constant and number of binding sites at different temperatures were measured. The thermodynamic parameters obtained at different temperatures showed van der Waals interactions and hydrogen bonds played the main roles in the interaction of myricetin with trypsin and lysozyme, hydrophobic force was dominant both in myricetin with α-chymotrypsin interaction and dihydromyricetin with trypsin and lysozyme interaction, as for the electrostatic forces, it was mainly the driving force in dihydromyricetin binding to α-chymotrypsin. There was non-radiative energy transfer between three proteinases and myricetin or dihydromyricetin with high probability. The microenvironment of trypsin, α-chymotrypsin and lysozyme is changed. The docking studies revealed that myricetin and dihydromyricetin entered the hydrophobic cavity of three proteinases and formed hydrogen bonds. The binding affinity of myricetin or dihydromyricetin is different with the trypsin, α-chymotrypsin and lysozyme due to the different molecular structure.

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Interaction mechanisms and structure-affinity relationships between hyperoside and soybean β-conglycinin and glycinin

Cited by 63 publications

References 38 publications

Exciton–tryptophan coupling pulse behaviour along with corona formation, binding analysis, and interaction study of ZnO nanorod–serum albumin protein bioconjugate

Exciton–tryptophan coupling pulse behaviour along with corona formation, binding analysis, and interaction study of ZnO nanorod–serum albumin protein bioconjugate

Ultrasound-assisted pH-shifting remodels egg-yolk low-density lipoprotein to enable construction of a stable aqueous solution of vitamin D3

Investigation on the interaction between myricetin and dihydromyricetin with trypsin, α‐chymotrypsin, lysozyme by spectroscopy and molecular docking methods

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