Surface plasmon resonance and circular dichroism characterization of cucurbitacins binding to serum albumins for early pharmacokinetic profiling

Fabini, Edoardo; Fiori, Giovana Maria Lanchoti; Tedesco, Daniele; Lopes, Norberto Peporine; Bertucci, Carlo

doi:10.1016/j.jpba.2016.01.051

Cited by 22 publications

(5 citation statements)

References 35 publications

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“…Lable-free optical biosensor based on SPR has been extensively used to study kinetic behavior of anticancer leads binding target proteins [38, 39]. In this case, SPR method was used to extract both the kinetic and thermodynamic parameters during the binding interactions of anticancer leads with HSA.…”

Section: Resultsmentioning

confidence: 99%

Uncovering the molecular and physiological processes of anticancer leads binding human serum albumin: A physical insight into drug efficacy

Liu

Wang

2017

PLoS ONE

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Human serum albumin (HSA) has its ability to bind drug molecules and influence their efficacies. Although anticancer leads NSC48693 and NSC290956 functioned at the same mechanism, the drug efficacies were obviously distinct. To gain insight into the distinct drug efficacy, the molecular and physiological processes of anticancer leads binding HSA have been investigated via a combined experimental and theoretical approach. The binding site, as characterized by fluorescence quenching and molecular modeling, is found to be located at site II in subdomain III A for NSC48693 with tight binding and at site FA1 in subdomain I B for NSC290956 with negatively cooperative binding, respectively. As indicated by the thermodynamic analysis, NSC48693 binds to HSA with an enthalpy driven mechanism, while NSC290956 binding with HSA is entropically driven. The further kinetic analysis indicates that the association rates appear to be similar to these two anticancer leads, however, the dissociation rate of NSC48693 is approximately 5-fold slower than that of NSC290956. For NSC48693, the pharmacodynamic efficacy is less than that of NSC290956, while its pharmacokinetic behavior is better than that of NSC290956. These parameters influence the pharmacodynamic efficacy and pharmacokinetic behavior, which will give further impacts on drug efficacy in vivo.

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Section: Resultsmentioning

confidence: 99%

Uncovering the molecular and physiological processes of anticancer leads binding human serum albumin: A physical insight into drug efficacy

Liu

Wang

2017

PLoS ONE

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“…40 The association and/or dissociation of the studied analyte to the immobilized protein leads to changes in mass transfer and subsequently influence the refractive index at the surface layer. 41 Variation in the refractive index causes changes in the SPR signal (RU). It is possible to determine both association and dissociation rate constants (k a and k d ) separately.…”

Section: Discussionmentioning

confidence: 99%

Kinetic and thermodynamic study of beta-Boswellic acid interaction with Tau protein investigated by surface plasmon resonance and molecular modeling methods

et al. 2019

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Introduction: Beta-Boswellic acid (BBA) is a pentacyclic terpene which has been obtained from frankincense and its beneficial effects on neurodegenerative disorders such as Alzheimer's disease (AD) have been addressed. Methods: In the present study, thermodynamic and kinetic aspects of BBA interaction with Tau protein as one of the important proteins involved in AD in the absence and presence of glucose has been investigated using surface plasmon resonance (SPR) method. Tau protein was immobilized onto the carboxy methyl dextran chip and its binding interactions with BBA were studied at physiological pH at various temperatures. Glucose interference with these interactions was also investigated. Results: Results showed that BBA forms a stable complex with Tau (K D =8.45×10 -7 M) at 298 K. Molecular modeling analysis showed a hydrophobic interaction between BBA and HVPGGG segment of R 2 and R 4 repeated domains of Tau. Conclusion: The binding affinity increased by temperature enhancement, while it decreased significantly in the presence of glucose. Both association and dissociation of the BBA-Tau complex were accompanied with an entropic activation barrier; however, positive enthalpy and entropy changes revealed that hydrophobic bonding is the main force involved in the interaction.

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“…Another partner in solution is placed together with the sensor. Fabini et al developed a sensor chip whose serum albumins were covalently bound to the carboxymethyl dextran layer of the sensor chips through its primary amine groups by an amine coupling reaction [ 111 ]. The result indicated that cucurbitacins were able to modulate the binding of biliverdin and serum albumins.…”

Section: Methods To Investigate the Interaction Between Active Herbalmentioning

confidence: 99%

Study on the interaction between active components from traditional Chinese medicine and plasma proteins

Jiao

Wang

Jiang

et al. 2018

Chemistry Central Journal

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Traditional Chinese medicine (TCM), as a unique form of natural medicine, has been used in Chinese traditional therapeutic systems over two thousand years. Active components in Chinese herbal medicine are the material basis for the prevention and treatment of diseases. Research on drug-protein binding is one of the important contents in the study of early stage clinical pharmacokinetics of drugs. Plasma protein binding study has far-reaching influence on the pharmacokinetics and pharmacodynamics of drugs and helps to understand the basic rule of drug effects. It is important to study the binding characteristics of the active components in Chinese herbal medicine with plasma proteins for the medical science and modernization of TCM. This review summarizes the common analytical methods which are used to study the active herbal components-protein binding and gives the examples to illustrate their application. Rules and influence factors of the binding between different types of active herbal components and plasma proteins are summarized in the end. Finally, a suggestion on choosing the suitable technique for different types of active herbal components is provided, and the prospect of the drug-protein binding used in the area of TCM research is also discussed.

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Surface plasmon resonance and circular dichroism characterization of cucurbitacins binding to serum albumins for early pharmacokinetic profiling

Cited by 22 publications

References 35 publications

Uncovering the molecular and physiological processes of anticancer leads binding human serum albumin: A physical insight into drug efficacy

Uncovering the molecular and physiological processes of anticancer leads binding human serum albumin: A physical insight into drug efficacy

Kinetic and thermodynamic study of beta-Boswellic acid interaction with Tau protein investigated by surface plasmon resonance and molecular modeling methods

Study on the interaction between active components from traditional Chinese medicine and plasma proteins

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