Specific interaction of chalcone-protein: Cardamonin binding site II on the human serum albumin molecule

Biopolymers ◽  
2005 ◽  
Vol 79 (1) ◽  
pp. 48-57 ◽  
Author(s):  
Wenying He ◽  
Ying Li ◽  
Jiaqin Liu ◽  
Zhide Hu ◽  
Xingguo Chen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Specific Interaction ◽  
Albumin Molecule ◽  
Human Serum Albumin Molecule

scholarly journals Fungicide Tebuconazole Influences the Structure of Human Serum Albumin Molecule

Molecules ◽  
2019 ◽  
Vol 24 (17) ◽  
pp. 3190 ◽  
Author(s):  
Katarína Želonková ◽  
Samuel Havadej ◽  
Valéria Verebová ◽  
Beáta Holečková ◽  
Jozef Uličný ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Spectra ◽  
Spectroscopic Techniques ◽  
Binding Modes ◽  
Conformation Changes ◽  
Relevant Role ◽  
Albumin Molecule ◽  
Human Serum Albumin Molecule

Studies of interactions between pesticides and target mammalian proteins are important steps toward understanding the pesticide′s toxicity. Using calorimetric and spectroscopic methods, the interaction between triazole fungicide tebuconazole and human serum albumin has been investigated. The spectroscopic techniques showed that fluorescence quenching of human serum albumin by tebuconazole was the result of the formation of tebuconazole/human serum albumin complex with the static type as the dominant mechanism. The association constant was found to be 8.51 × 103 L/mol. The thermodynamic parameters were obtained as ΔH = −56.964 kJ/mol, ΔS = −115.98 J/mol·K. The main active interactions forming the tebuconazole/human serum albumin complex were identified as the interplay between hydrogen bonds and/or van der Waals forces, based on thermodynamic experiments. These binding modes were corroborated well by the predictions of molecular modeling. Hydrogen bonding of tebuconazole with Arg222, Ala215 and Ala291 of human serum albumin played a relevant role in binding. The conformation changes in secondary structure were characterized by circular dichroism and 3D fluorescence spectra.

scholarly journals Effect of the binding of bilirubin to either the first class or the second class of binding sites of the human serum albumin molecule on its photochemical reaction

1989 ◽  
Vol 257 (3) ◽  
pp. 711-714 ◽  
Author(s):  
S Onishi ◽  
S Itoh ◽  
K Isobe ◽  
M Ochi ◽  
T Kunikata ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Serum Bilirubin ◽  
Bilirubin Concentration ◽  
Kinetics Of ◽  
Albumin Molecule ◽  
Human Serum Albumin Molecule ◽  
Serum Bilirubin Concentration

The kinetics of the photochemical changes of bilirubin were studied at a constant concentration of bilirubin bound either to the first class or to the second class of binding sites of the human serum albumin molecule. The more the bilirubin binds to the first class of binding sites in the human serum albumin molecule, the more readily geometric photoequilibrium to give (ZE)-bilirubin takes place. The more the bilirubin binds to the second class of binding sites or allosterically transformed binding sites induced by added SDS, the more readily structural photoisomerization, i.e. the formation of (EZ)-cyclobilirubin, takes place. When the serum bilirubin concentration is at low, safe, values bilirubin binds exclusively to the first class of binding sites and serves as an antioxidant [Onishi, Yamakawa & Ogawa (1971) Perinatology 1, 373-379]; at these concentrations human serum albumin protects bilirubin from irreversible photodegradation by only allowing readily reversible geometric photoisomerization. As the serum bilirubin concentration increases to high, and potentially dangerous, values, bilirubin binds to the second class of binding sites, and under these conditions human serum albumin seems to promote the photocyclization of bilirubin. During irradiation human serum albumin seems to act by retaining low, useful, concentrations of bilirubin while facilitating irreversible photoisomerization of excess bilirubin.

scholarly journals Dansylation of human serum albumin in the study of the primary binding sites of bilirubin and l-tryptophan

1979 ◽  
Vol 181 (1) ◽  
pp. 251-253 ◽  
Author(s):  
C Jacobsen ◽  
J Jacobsen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Binding Sites ◽  
Lysine Residue ◽  
Bilirubin Binding ◽  
Albumin Molecule ◽  
Common Cavity

Binding of bilirubin and of L-tryptophan to dansylated albumins was investigated. Dansylation of less than one lysine residue per molecule of albumin did not affect the bilirubin binding, but decreased the L-tryptophan binding, indicating that dansylation had taken place in or near the l-tryptophan-binding site. Native albumin and albumin-bilirubin 1:1 complex showed the same affinity for L-tryptophan. The results indicate that, although L-tryptophan and bilirubin are bound in the same region, perhaps in a common cavity of the albumin molecule, such a cavity is sufficiently large to contain both ligands.

scholarly journals Indomethacin Increases Quercetin Affinity for Human Serum Albumin: A Combined Experimental and Computational Study and Its Broader Implications

2020 ◽  
Vol 21 (16) ◽  
pp. 5740
Author(s):  
Hrvoje Rimac ◽  
Tana Tandarić ◽  
Robert Vianello ◽  
Mirza Bojić
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Binding Sites ◽  
Quantum Chemical ◽  
Computational Study ◽  
The Body ◽  
Active Concentration ◽  
Insight Into

Human serum albumin (HSA) is the most abundant carrier protein in the human body. Competition for the same binding site between different ligands can lead to an increased active concentration or a faster elimination of one or both ligands. Indomethacin and quercetin both bind to the binding site located in the IIA subdomain. To determine the nature of the HSA-indomethacin-quercetin interactions, spectrofluorometric, docking, molecular dynamics studies, and quantum chemical calculations were performed. The results show that the indomethacin and quercetin binding sites do not overlap. Moreover, the presence of quercetin does not influence the binding constant and position of indomethacin in the pocket. However, binding of quercetin is much more favorable in the presence of indomethacin, with its position and interactions with HSA significantly changed. These results provide a new insight into drug-drug interactions, which can be important in situations when displacement from HSA or other proteins is undesirable or even desirable. This principle could also be used to deliberately prolong or shorten the xenobiotics’ half-life in the body, depending on the desired outcomes.

Interaction of an anticancer drug, gefitinib with human serum albumin: insights from fluorescence spectroscopy and computational modeling analysis

RSC Advances ◽  
2016 ◽  
Vol 6 (94) ◽  
pp. 91756-91767 ◽  
Author(s):  
Md. Zahirul Kabir ◽  
Wei-Ven Tee ◽  
Saharuddin B. Mohamad ◽  
Zazali Alias ◽  
Saad Tayyab
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Spectroscopy ◽  
Serum Albumin ◽  
Computational Modeling ◽  
Human Serum ◽  
Binding Site ◽  
Anticancer Drug ◽  
Modeling Analysis ◽  
Binding Orientation

Binding orientation of the GEF in the binding site III, located in subdomain IB of HSA.

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