scholarly journals Bioactive anthraquinones found in plant foods interact with human serum albumin and inhibit the formation of advanced glycation endproducts

2018 ◽  
Vol 4 ◽  
Author(s):  
Weixi Liu ◽  
Ang Cai ◽  
Rachel Carley ◽  
Robert Rocchio ◽  
Zoe M. Petrovas ◽  
...  
Keyword(s):  
Protein Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Advanced Glycation Endproducts ◽  
Critical Role ◽  
Titration Calorimetry ◽  
Vis Spectroscopy ◽  
Anthraquinone Derivatives ◽  
Aloe Emodin

The glycation of human serum albumin (HSA) plays a critical role in the development of many disorders. Herein, the anti-glycation effects of several natural dietary anthraquinone derivatives including aloin, aloe-emodin, chrysophanol, emodin, physcion, and rhein were evaluated. The anthraquinones at 100 μM reduced fructose-, methylglyoxal-, and glyoxal-induced HSA glycation by 21% (aloe-emodin) to 92% (aloin), 17% (physcion) to 94% (emodin), and 16% (anthraquinone) to 67% (emodin), respectively. These anthraquinone derivatives also protected HSA by maintaining its free amino acid residues and secondary protein structure as characterized by circular dichroism. The mechanisms of their anti-glycation effects were investigated using rhein as a representative anthraquinone. The interactions between rhein and HSA were evaluated by biophysical characterizations, namely, isothermal titration calorimetry and UV-vis spectroscopy as well as computational modeling. Our findings suggest that the anti-glycation effects of these anthraquinones may be attributed to their binding capacity and stabilization of the HSA protein structure.

Investigation of the Effects of Various Cyclodextrins on the Stabilisation of Human Serum Albumin by a Spectroscopic Method

2015 ◽  
Vol 68 (12) ◽  
pp. 1894 ◽  
Author(s):  
Mohsen Oftadeh ◽  
Golamreza Rezaei Behbahani ◽  
Ali Akbar Saboury ◽  
Shahnaz Rafiei
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Electrostatic Interactions ◽  
Spectroscopic Method ◽  
Phosphate Buffer Solution ◽  
Blue Shift ◽  
Titration Calorimetry ◽  
Tryptophan Residue ◽  
Buffer Solution

The binding parameters between cyclodextrins (CDs) and human serum albumin (HSA) were investigated by isothermal titration calorimetry (ITC), fluorescence quenching, and UV-vis absorption spectroscopy at 300 K in 50 mM phosphate buffer solution. Among the various CDs investigated, β-CD has the greater ability to decrease the aggregation of HSA and the results indicated that the inhibition order is γ-CD < α-CD < β-CD. The obtained heats for HSA+CDs interactions were reported and analysed in terms of the extended solvation model, which was used to reproduce the enthalpies of HSA interactions with CDs over a broad range of complex concentrations. The binding constant and thermodynamic parameters were obtained. These suggested that the binding reaction was driven by both enthalpy and entropy, and electrostatic interactions played a major role in the stabilising of HSA. The parameters and reflected the net effect of β-CD on the HSA stability at low and high cyclodextrin concentrations, respectively. The positive values for indicated that β-CD stabilises the HSA structure at low concentrations. The UV absorption intensity of theses complexes increased and a slight red shift was observed in the absorbance wavelength with increasing the CD concentration. The fluorescence intensity of HSA decreased regularly and a slight blue shift was observed for the emission wavelength with increasing CD concentration. The results indicate that the CD complex could quench the fluorescence of HSA and changes the microenvironment of the tryptophan residue.

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.

Localization of Tolbutamide Binding Sites on Human Serum Albumin Using Titration Calorimetry and Heteronuclear 2-D NMR

Biochemistry ◽  
1995 ◽  
Vol 34 (27) ◽  
pp. 8780-8787 ◽  
Author(s):  
Michael G. Jakoby ◽  
Douglas F. Covey ◽  
David P. Cistola
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Titration Calorimetry

scholarly journals A Comparative Interaction between Copper Ions with Alzheimer'sβAmyloid Peptide and Human Serum Albumin

2012 ◽  
Vol 2012 ◽  
pp. 1-4 ◽  
Author(s):  
G. Rezaei Behbehani ◽  
L. Barzegar ◽  
M. Mohebbian ◽  
A. A. Saboury
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Copper Ions ◽  
Copper Ion ◽  
Titration Calorimetry ◽  
Solvation Model ◽  
Solvation Parameters ◽  
Induced Aggregation

The interaction of Cu2+with the first 16 residues of the Alzheimer's amyliodβpeptide,Aβ(1–16), and human serum albumin (HSA) were studied in vitro by isothermal titration calorimetry at pH 7.2 and 310 K in aqueous solution. The solvation parameters recovered from the extended solvation model indicate that HSA is involved in the transport of copper ion. Complexes betweenAβ(1–16) and copper ions have been proposed to be an aberrant interaction in the development of Alzheimer's disease, where Cu2+is involved inAβ(1–16) aggregation. The indexes of stability indicate that HSA removed Cu2+fromAβ(1–16), rapidly, decreased Cu-induced aggregation ofAβ(1–16), and reduced the toxicity ofAβ(1–16) + Cu2+significantly.

The critical role of dimer formation in monosaccharides binding to human serum albumin

2018 ◽  
Vol 20 (5) ◽  
pp. 3249-3257 ◽  
Author(s):  
Prapasiri Pongprayoon ◽  
Toshifumi Mori
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Critical Role ◽  
Binding Pocket ◽  
Dimer Formation ◽  
Dimeric Structure

Monosaccharides are found to bind tightly to human serum albumin when a dimeric structure is formed in the binding pocket.

At very low concentrations known chaotropes act as kosmotropes for the N and B isoforms of human serum albumin

2013 ◽  
Vol 91 (2) ◽  
pp. 72-78 ◽  
Author(s):  
Priyankar Sen ◽  
Mohd Moin Khan ◽  
Asif Equbal ◽  
Ejaz Ahmad ◽  
Rizwan Hasan Khan
Keyword(s):  
Protein Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Electrostatic Interaction ◽  
Tertiary Structure ◽  
Guanidine Hydrochloride ◽  
Micelle Formation ◽  
Low Concentrations ◽  
Secondary And Tertiary Structure

Very few studies have been done to understand the effect of millimolar concentrations of chaotropes on protein structure. In our previous study we observed that the secondary and tertiary structure of human serum albumin (HSA) increases in the presence of 5 mmol/L urea. Micelle formation in amphoteric detergents increases in the presence of equivalent concentrations of urea. Here, we observed a significant increase in the secondary and tertiary structure of HSA. Interestingly, guanidine hydrochloride, another chaotropic agent, also shows a similar effect. Our results show electrostatic interaction may play a role in neutral to basic transition in HSA. This study further supports the claim that at millimolar concentrations the chaotropes may act as kosmotropes for proteins.

DENATURATION OF HUMAN SERUM ALBUMIN BY CERIUM (III) CHLORIDE

2013 ◽  
Vol 08 (01n02) ◽  
pp. 59-71
Author(s):  
G. REZAEI BEHBAHANI ◽  
M. SHALBAFAN ◽  
N. GHEIBI ◽  
L. BARZEGAR ◽  
H. REZAEI BEHBAHANI ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Changes ◽  
Tertiary Structure ◽  
Fluorescence Emission ◽  
Titration Calorimetry ◽  
Tryptophan Residue ◽  
Spectroscopic Methods ◽  
Irreversible Denaturation

Cerium (III) Chloride-induced conformational changes of human serum albumin, HSA, in phosphate buffer, 10 mM at pH 7.4 was investigated, using isothermal titration calorimetry (ITC), UV and fluorescence emission spectroscopic methods. The results indicate that CeCl3, Ce3+, induces irreversible denaturation of the HSA structure. The UV absorption intensity of HSA + Ce3+ shows a slight blueshift in the absorbance wavelength with increasing Ce3+ concentration. The fluorescence intensity was increased regularly and a slight redshift was observed in the emission wavelength. The HSA + Ce3+ complex quenches the fluorescence of HSA and changes the microenvironment of tryptophan residue. The emission intensity increases suggesting the loss of the tertiary structure of HSA. The results obtained from the ITC data are in agreement with the spectroscopic methods. The strong negative cooperativity of Ce3+ binding with HSA (Table 1) recovered from the extended solvation model, indicates that HSA has been denatured as a result of its interaction with Ce3+ ions.

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