Investigation of the interaction between flavonoids and human serum albumin

Bi, Shuyun; Ding, Lan; Tian, Yuan; Song, Daqian; Zhou, Xin; Liu, Xia; Zhang, Hanqi

doi:10.1016/j.molstruc.2004.05.026

Cited by 411 publications

(164 citation statements)

References 9 publications

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“…When small molecules bind independently to a set of equivalent sites on a macromolecule and the equilibrium between the free and the bound molecules has been reached, the fluorescence intensities obey the following equation [34,35]:…”

Section: Binding Parametersmentioning

confidence: 99%

Probing the binding mechanisms of α-tocopherol to trypsin and pepsin using isothermal titration calorimetry, spectroscopic, and molecular modeling methods

2016

J Biol Phys

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α-Tocopherol is a required nutrient for a variety of biological functions. In this study, the binding of α-tocopherol to trypsin and pepsin was investigated using isothermal titration calorimetry (ITC), steady-state and time-resolved fluorescence measurements, circular dichroism (CD) spectroscopy, and molecular modeling methods. Thermodynamic investigations reveal that α-tocopherol binds to trypsin/pepsin is synergistically driven by enthalpy and entropy. The fluorescence experimental results indicate that α-tocopherol can quench the fluorescence of trypsin/pepsin through a static quenching mechanism. The binding ability of α-tocopherol with trypsin/pepsin is in the intermediate range, and one molecule of α-tocopherol combines with one molecule of trypsin/pepsin. As shown by circular dichroism (CD) spectroscopy, α-tocopherol may induce conformational changes of trypsin/pepsin. Molecular modeling displays the specific binding site and gives information about binding forces and α-tocopherol-tryptophan (Trp)/tyrosine (Tyr) distances. In addition, the inhibition rate of α-tocopherol on trypsin and pepsin was studied. The study provides a basic data set for clarifying the binding mechanisms of α-tocopherol with trypsin and pepsin and is helpful for understanding its biological activity in vivo.

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Section: Binding Parametersmentioning

confidence: 99%

Probing the binding mechanisms of α-tocopherol to trypsin and pepsin using isothermal titration calorimetry, spectroscopic, and molecular modeling methods

2016

J Biol Phys

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“…For the static quenching, when small molecules bind independently to a set of equivalent sites on a macromolecule, the equilibrium between free and bound molecules could be Table 2 The binding constant K a and relative thermodynamic parameters of the flavonoid-hyaluronidase systems (n=3) represented by the following equation [38]: Fig. 4), the number binding sites n and binding constant K a of the interaction between HAase and flavonoids can be calculated and the results are summarized in Table 2.…”

Section: Binding Constant and The Number Of Binding Sitesmentioning

confidence: 99%

Molecular Interactions of Flavonoids to Hyaluronidase: Insights from Spectroscopic and Molecular Modeling Studies

Zeng

Yang

et al. 2015

J Fluoresc

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In the work described on this paper, the interactions between eight flavonoids and hyaluronidase (HAase), an important enzyme involved in a promoting inflammation pathway, were investigated by spectroscopic and molecular modeling methods. The results revealed that all flavonoids could interact with HAase to form flavonoid-HAase complexes. The binding parameters obtained from the data at different temperatures indicated that flavonoids could spontaneously bind with HAase mainly through electrostatic forces and hydrophobic interactions with one binding site. According to synchronous and three-dimensional fluorescence spectra and the molecular docking results, all flavonoids bound directly into the enzyme cavity site and the binding of flavonoid into the enzyme cavity influenced the microenvironment of the HAase activity site which led to the reduced enzyme activity. The present study provides direct evidence at a molecular level to understand the mechanism of inhibitory effect of flavonoid against HAase and explain the anti-inflammatory mechanism of the Traditional Chinese Medicines as anti-inflammatory drugs.

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“…(21) Flavonoids are important effective constituents of some medicines, especially of Chinese herbal medicines, and showed a wide range of therapeutic activities against cancers, tumors, acquired immunodefi ciency syndrome, allergies, etc. (22)(23)(24) In addition to their antioxidant properties, fl avonoids have been reported to exhibit antiviral, antibacterial, anti-infl ammatory, vasodilatory, anticancer, and anti-ischemic activity. Moreover, they are also able to inhibit lipid peroxidation and platelet aggregation, and increase capillary permeability and fragility.…”

Section: Plants Have Been Used By Human Being Sincementioning

confidence: 99%

A Review on Pharmacological and Analytical Aspects of Naringenin

Patel

Singh

Patel

2014

Chin. J. Integr. Med.

189

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Flavonoids are a widely distributed group of phytochemicals having benzo-pyrone nucleus, and more than 4,000 different flavonoids have been described and categorized into flavonols, flavones, flavanones, isoflavones, catechins and anthocyanidins. Flavonoids occurs naturally in fruits, vegetables, nuts, and beverages such as coffee, tea, and red wine, as well as in medical herbs. Flavonoids are responsible for the different colors of plant parts and are important constituents of the human diet. Flavanoids have different pharmacological activities, such as antioxidant, anti-allergic, antibacterial, anti-inflammatory, antimutagenic and anticancer activity. Naringenin belongs to the flavanones and is mainly found in fruits (grapefruit and oranges) and vegetables. Pharmacologically, it has anticancer, antimutagenic, anti-inflammatory, antioxidant, antiproliferative and antiatherogenic activities. Naringenin is used for the treatments of osteoporosis, cancer and cardiovascular diseases, and showed lipid-lowering and insulin-like properties. In the present review, detailed pharmacological and analytical aspects of naringenin have been presented, which revealed the impressive pharmacological profile and the possible usefulness in the treatment of different types of diseases in the future. The information provided in this communication will act as an important source for development of effective medicines for the treatment of various disorders.

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Investigation of the interaction between flavonoids and human serum albumin

Cited by 411 publications

References 9 publications

Probing the binding mechanisms of α-tocopherol to trypsin and pepsin using isothermal titration calorimetry, spectroscopic, and molecular modeling methods

Probing the binding mechanisms of α-tocopherol to trypsin and pepsin using isothermal titration calorimetry, spectroscopic, and molecular modeling methods

Molecular Interactions of Flavonoids to Hyaluronidase: Insights from Spectroscopic and Molecular Modeling Studies

A Review on Pharmacological and Analytical Aspects of Naringenin

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