Abstract:The green Brazilian bay leaf, a spice much prized in local cuisine (Aniba riparia, Lauraceae), contains chemical compounds presenting benzoyl-derivatives named riparins, which have anti-inflammatory, antimicrobial and anxiolytic properties. However, it is unclear what kind of interaction riparins perform with any molecular target. As a profitable target, human serum albumin (HSA) is one of the principal extracellular proteins, with an exceptional capacity to interact with several molecules, and it also plays a… Show more
“…The K a for the three temperatures remained close to the order of magnitude of 10 4 M −1 . According to the literature, this meant that the binding constant was moderate for the albumin proteins from different species [32,33,34]. The number of sites, n, remained close to the unity, which was in concordance with the first order binding equilibrium model.…”
Section: Resultssupporting
confidence: 72%
“…Such methods (binding equilibrium model and IDF) showed that, although the results obtained were in the same order of magnitude for the binding constant 10 4 M −1 , the same could not be said about the number of sites. Such results showed that both methods had reasonable agreement, revealing that the complex had an affinity constant that relayed between 10 4 –10 6 M −1 , which was a moderate constant for most of the albumin proteins [32,33,34]. Although the binding constant (K b ) obtained from the Scatchard plot had the same order of magnitude of K a obtained from the double log plot, the difference between the number of binding sites indicated that the IDF method was more realistic.…”
Section: Resultsmentioning
confidence: 96%
“…By comparing the values obtained between enthalpy and entropy, it could be seen that the enthalpy contribution was more significant. This showed that interactions of the type hydrogen bonds and the Van der Waals force were most likely playing the main role in the stabilization of the complex [34,35,36,37].…”
The bioactive piperine (1-piperoyl piperidine) compound found in some pepper species (Piper nigrum linn and Piper sarmentosum Roxb) has been shown to have therapeutic properties and to be useful for well-being. The tests used to validate these properties were performed in vitro or with small rats. However, in all these assays, the molecular approach was absent. Although the first therapeutic trials relied on the use of rats, no proposal was mentioned either experimentally or computationally at the molecular level regarding the interaction between piperine and rat serum albumin (RSA). In the present study, several spectroscopic techniques were employed to characterize rat serum albumin and, aided by computational techniques, the protein modeling was proposed. From the spectroscopic results, it was possible to estimate the binding constant (3.9 × 104 M−1 at 288 K) using the Stern–Volmer model and the number of ligands (three) associated with the protein applying interaction density function model. The Gibbs free energy, an important thermodynamic parameter, was determined (−25 kJ/mol), indicating that the interaction was spontaneous. This important set of experimental results served to parameterize the computational simulations. The results of molecular docking and molecular dynamics matched appropriately made it possible to have detailed microenvironments of RSA accessed by piperine.
“…The K a for the three temperatures remained close to the order of magnitude of 10 4 M −1 . According to the literature, this meant that the binding constant was moderate for the albumin proteins from different species [32,33,34]. The number of sites, n, remained close to the unity, which was in concordance with the first order binding equilibrium model.…”
Section: Resultssupporting
confidence: 72%
“…Such methods (binding equilibrium model and IDF) showed that, although the results obtained were in the same order of magnitude for the binding constant 10 4 M −1 , the same could not be said about the number of sites. Such results showed that both methods had reasonable agreement, revealing that the complex had an affinity constant that relayed between 10 4 –10 6 M −1 , which was a moderate constant for most of the albumin proteins [32,33,34]. Although the binding constant (K b ) obtained from the Scatchard plot had the same order of magnitude of K a obtained from the double log plot, the difference between the number of binding sites indicated that the IDF method was more realistic.…”
Section: Resultsmentioning
confidence: 96%
“…By comparing the values obtained between enthalpy and entropy, it could be seen that the enthalpy contribution was more significant. This showed that interactions of the type hydrogen bonds and the Van der Waals force were most likely playing the main role in the stabilization of the complex [34,35,36,37].…”
The bioactive piperine (1-piperoyl piperidine) compound found in some pepper species (Piper nigrum linn and Piper sarmentosum Roxb) has been shown to have therapeutic properties and to be useful for well-being. The tests used to validate these properties were performed in vitro or with small rats. However, in all these assays, the molecular approach was absent. Although the first therapeutic trials relied on the use of rats, no proposal was mentioned either experimentally or computationally at the molecular level regarding the interaction between piperine and rat serum albumin (RSA). In the present study, several spectroscopic techniques were employed to characterize rat serum albumin and, aided by computational techniques, the protein modeling was proposed. From the spectroscopic results, it was possible to estimate the binding constant (3.9 × 104 M−1 at 288 K) using the Stern–Volmer model and the number of ligands (three) associated with the protein applying interaction density function model. The Gibbs free energy, an important thermodynamic parameter, was determined (−25 kJ/mol), indicating that the interaction was spontaneous. This important set of experimental results served to parameterize the computational simulations. The results of molecular docking and molecular dynamics matched appropriately made it possible to have detailed microenvironments of RSA accessed by piperine.
“…To us this suggests that many of the citing authors have not read our article in sufficient detail, or did not understand it. In connection to the double log equation alone, we found seven more publications that inappropriately cite our paper unequivocally and directly in support of their use and/or interpretation of the double log equation in terms of the number of binding sites [8][9][10][11][12][13][14]. We do note that one of these articles, upon our request, has been corrected, in the sense that the inappropriate reference to our work in support of the double log equation has been removed [14].…”
“…The binding constant ( K b ) and the number of binding sites ( n ) of Pyr and 1-OHPyr with BSA in binary and ternary interaction systems could be calculated by fitting the curve based on Eq. (2) [3] , [4] . Fig.…”
This article present data related to the publication entitled “Interactions of pyrene and/or 1-hydroxypyrene with bovine serum albumin based on EEM-PARAFAC combined with molecular docking” (Zhang et al., 2018) [1]. The excitation-emission matrix (EEM) fluorescence spectral parameters of pyrene, 1-hydroxypyrene, bovine serum albumin (BSA), and their mixtures were presented in this article. Combined EEM - parallel factor analysis with fluorescence quenching analysis, some data related to the binding affinity of pyrene and/or 1-hydroxypyrene with BSA in the binary and ternary systems were obtained.
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