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Journal ArticleDOI

Interaction of fisetin with human serum albumin by fluorescence, circular dichroism spectroscopy and DFT calculations: binding parameters and conformational changes

Iulia Matei, +2 more
- 01 Aug 2011 - 
- Vol. 131, Iss: 8, pp 1629-1635
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TLDR
In this paper, the interaction between fisetin, an antioxidant and neuroprotective flavonoid, and human serum albumin (HSA) was investigated by means of fluorescence (steadystate, synchronous, time-resolved) and circular dichroism (CD) spectroscopy.
About
This article is published in Journal of Luminescence.The article was published on 2011-08-01. It has received 58 citations till now. The article focuses on the topics: Circular dichroism & Human serum albumin.

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Citations
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DNA- and BSA-binding studies and anticancer activity against human breast cancer cells (MCF-7) of the zinc(II) complex coordinated by 5,6-diphenyl-3-(2-pyridyl)-1,2,4-triazine.

TL;DR: The results indicate that the parent complex displays cytotoxicity against human breast cancer cell lines (MCF-7) with an IC50 value of 10.44μM, remarkable that the complex can introduce as a potential anticancer drug.
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Spectroscopic studies on the interaction between tetrandrine and two serum albumins by chemometrics methods.

TL;DR: The results of synchronous fluorescence, 3D fluorescence and FT-IR spectra show that the conformation of proteins has altered in the presence of tetrandrine, and the binding of TETD-HSA was strongly relied on the hydrophobic interaction.
Journal ArticleDOI

Binding of Phthalate Plasticizers to Human Serum Albumin in Vitro: A Multispectroscopic Approach and Molecular Modeling

TL;DR: The thermodynamic analysis implied that hydrophobic forces were the main interaction for the plasticizers-HSA system, which agreed well with the results from the molecular modeling study, and the alterations of HSA secondary structure in the presence of phthalate plasticizers.
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Studies on the interaction between scopoletin and two serum albumins by spectroscopic methods

TL;DR: In this paper, the interactions of scopoletin to bovine serum albumin (BSA) and HSA have been investigated by using spectroscopic methods.
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A review on structure-affinity relationship of dietary flavonoids with serum albumins.

TL;DR: The present review summarizes the interactions of flavonoids categorized as flavanol, flavonol, flavone, isoflavone, flavanones, and anthocyanidins with SAs and finds that catechin gallates have higher binding affinity to SAs than catechins and gallocatechins and inorganic metal ions modulate the binding affinity.
References
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Book

Principles of fluorescence spectroscopy

TL;DR: This book describes the fundamental aspects of fluorescence, the biochemical applications of this methodology, and the instrumentation used in fluorescence spectroscopy.
Journal ArticleDOI

The Attractions of Proteins for Small Molecules and Ions

TL;DR: The number and variety of known compounrjs between proteins and small molecules are increasing rapidly and make a fascinating story as discussed by the authors, and there are many compounds of serum albumin, which was used during the war by many chemists, most of whom found at least one 6ew compound.
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Thermodynamics of protein association reactions: forces contributing to stability

Philip D. Ross, +1 more
- 26 May 1981 - 
TL;DR: On the basis of the thermochemical behavior of small molecule interactions, it is concluded that the strengthening of hydrogen bonds in the past decade, a complete thermodynamic description of the self-association of many proteins and their interactions is concluded.
BookDOI

Molecular fluorescence : principles and applications

TL;DR: In this article, the effects of intermolecular photophysical processes on fluorescence emission are discussed and an analysis of the effect of polarity of fluorescence emissions is presented.
Journal ArticleDOI

Atomic structure and chemistry of human serum albumin.

TL;DR: The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 Å and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serumalbumin.