Fluorescence studies by quenching and protein unfolding on the interaction of bioactive compounds in water extracts of kiwi fruit cultivars with human serum albumin

2015 ◽  
Vol 160 ◽  
pp. 71-77 ◽  
Author(s):  
Yong Seo Park ◽  
Martin Polovka ◽  
Alma Leticia Martinez-Ayala ◽  
Gustavo A. González-Aguilar ◽  
Kyung-Sik Ham ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Bioactive Compounds ◽  
Protein Unfolding ◽  
Kiwi Fruit ◽  
Fluorescence Studies ◽  
Water Extracts

scholarly journals Insight of the Interaction between 2,4-thiazolidinedione and Human Serum Albumin: A Spectroscopic, Thermodynamic and Molecular Docking Study

2019 ◽  
Vol 20 (11) ◽  
pp. 2727 ◽  
Author(s):  
Safikur Rahman ◽  
Md Tabish Rehman ◽  
Gulam Rabbani ◽  
Parvez Khan ◽  
Mohamed F AlAjmi ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Docking Study ◽  
Dynamics Simulation ◽  
Titration Calorimetry ◽  
Peroxisome Proliferator ◽  
Molecular Docking Study ◽  
Fluorescence Studies

Thiazolidinedione derivatives (TZDs) have attracted attention because of their pharmacological effects. For example, certain TZDs have been reported to ameliorate type II diabetes by binding and activating PPARs (peroxisome proliferator-activated receptors). Nonetheless, no information is available on the interaction between the heterocyclic 2, 4-thiazolidinedione (2,4-TZD) moiety and serum albumin, which could affect the pharmacokinetics and pharmacodynamics of TZDs. In this study, we investigated the binding of 2,4-TZD to human serum albumin (HSA). Intrinsic fluorescence spectroscopy revealed a 1:1 binding stoichiometry between 2,4-TZD and HSA with a binding constant (Kb) of 1.69 ± 0.15 × 103 M−1 at 298 K. Isothermal titration calorimetry studies showed that 2,4-TZD/HSA binding was an exothermic and spontaneous reaction. Molecular docking analysis revealed that 2,4-TZD binds to HSA subdomain IB and that the complex formed is stabilized by van der Waal’s interactions and hydrogen bonds. Molecular dynamics simulation confirmed the stability of the HSA-TZD complex. Further, circular dichroism and 3D fluorescence studies showed that the global conformation of HSA was slightly altered by 2,4-TZD binding, enhancing its stability. The results obtained herein further help in understanding the pharmacokinetic properties of thiazolidinedione.

Time-resolved fluorescence studies on site-directed mutants of human serum albumin

FEBS Letters ◽  
1997 ◽  
Vol 408 (1) ◽  
pp. 67-70 ◽  
Author(s):  
Michael K Helms ◽  
Charles E Petersen ◽  
Nadhipuram V Bhagavan ◽  
David M Jameson
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Fluorescence Studies

The Effects of Drug Complexation on the Stability and Conformation of Human Serum Albumin: Protein Unfolding

2006 ◽  
Vol 45 (2) ◽  
pp. 203-214 ◽  
Author(s):  
A. Ahmed-Ouameur ◽  
S. Diamantoglou ◽  
M. R. Sedaghat-Herati ◽  
Sh. Nafisi ◽  
R. Carpentier ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Protein Unfolding ◽  
The Stability

scholarly journals Enantioresolution and Binding Affinity Studies on Human Serum Albumin: Recent Applications and Trends

Chemosensors ◽  
2021 ◽  
Vol 9 (11) ◽  
pp. 304
Author(s):  
Tony Cardoso ◽  
Ana Sofia Almeida ◽  
Fernando Remião ◽  
Carla Fernandes
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Affinity ◽  
Bioactive Compounds ◽  
High Performance ◽  
Binding Studies ◽  
Chiral Drugs ◽  
Innovative Methods ◽  
Chemistry Research

The interaction between proteins and drugs or other bioactive compounds has been widely explored over the past years. Several methods for analysis of this phenomenon have been developed and improved. Nowadays, increasing attention is paid to innovative methods, such as high performance affinity liquid chromatography (HPALC) and affinity capillary electrophoresis (ACE), taking into account various advantages. Moreover, the development of separation methods for the analysis and resolution of chiral drugs has been an area of ongoing interest in analytical and medicinal chemistry research. In addition to bioaffinity binding studies, both HPALC and ACE al-low one to perform other type of analyses, namely, displacement studies and enantioseparation of racemic or enantiomeric mixtures. Actually, proteins used as chiral selectors in chromatographic and electrophoretic methods have unique enantioselective properties demonstrating suitability for the enantioseparation of a large variety of chiral drugs or other bioactive compounds. This review is mainly focused in chromatographic and electrophoretic methods using human serum albumin (HSA), the most abundant plasma protein, as chiral selector for binding affinity analysis and enantioresolution of drugs. For both analytical purposes, updated examples are presented to highlight recent applications and current trends.

Fluorescence studies of tryptophan and human serum albumin (HSA) in AOT micelles

1994 ◽  
Author(s):  
Daniel M. Davis ◽  
David McLoskey ◽  
David J. S. Birch ◽  
Ronald M. Swart ◽  
P. R. Gellert ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Studies

scholarly journals Molecular Basis of Interactions between the Antibiotic Nitrofurantoin and Human Serum Albumin: A Mechanism for the Rapid Drug Blood Transportation

2021 ◽  
Vol 22 (16) ◽  
pp. 8740
Author(s):  
Antonella Calderaro ◽  
Alessandro Maugeri ◽  
Salvatore Magazù ◽  
Giuseppina Laganà ◽  
Michele Navarra ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Biological Effects ◽  
Protein Secondary Structure ◽  
Ligand Docking ◽  
Fluorescence Studies ◽  
Biological Potential ◽  
Vis Spectroscopy

Nitrofurantoin is an antimicrobial agent obtained through the addition of a nitro group and a side chain containing hydantoin to a furan ring. The interactions of the antibiotic with human serum albumin (HSA) have been investigated by fluorescence, UV-VIS, Fourier transform infrared spectroscopy (FTIR) spectroscopy, and protein-ligand docking studies. The fluorescence studies indicate that the binding site of the additive involves modifications of the environment around Trp214 at the level of subdomain IIA. Fluorescence and UV-VIS spectroscopy, displacement studies, and FTIR experiments show the association mode of nitrofurantoin to HSA, suggesting that the primary binding site of the antibiotic is located in Sudlow’s site I. Molecular modeling suggests that nitrofurantoin is involved in the formation of hydrogen bonds with Trp214, Arg218, and Ser454, and is located in the hydrophobic cavity of subdomain IIA. Moreover, the curve-fitting results of the infrared Amide I’ band indicate that the binding of nitrofurantoin induces little change in the protein secondary structure. Overall, these data clarify the blood transportation process of nitrofurantoin and its rapid transfer to the kidney for its elimination, hence leading to a better understanding of its biological effects and being able to design other molecules, based on nitrofurantoin, with a higher biological potential.

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