Water-soluble noncovalent adducts of the heterometallic copper subgroup complexes and human serum albumin with remarkable luminescent properties

2014 ◽  
Vol 50 (7) ◽  
pp. 849-851 ◽  
Author(s):  
P. S. Chelushkin ◽  
D. V. Krupenya ◽  
Yu-Jui Tseng ◽  
Ting-Yi Kuo ◽  
Pi-Tai Chou ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Luminescent Properties ◽  
Water Soluble ◽  
Subgroup Complexes

Effect of aggregation of a cationic phthalocyanine in micelles and in the presence of human serum albumin

2006 ◽  
Vol 10 (01) ◽  
pp. 33-42 ◽  
Author(s):  
Myriam E. Rodriguez ◽  
Daniel A. Fernández ◽  
Josefina Awruch ◽  
Silvia E. Braslavsky ◽  
Lelia E. Dicelio
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Hydrophobic Interactions ◽  
Photophysical Properties ◽  
Sodium Dodecylsulfate ◽  
Water Soluble ◽  
Quantum Yields ◽  
Ionic Interactions ◽  
Triplet Quantum Yields

The photophysical properties of tetrakis(1,1-dimethyl-2-trimethylammonium)ethylphthalocyaninato zinc(II) tetraiodide (I) – a water-soluble cationic phthalocyanine – are presented in the presence of human serum albumin (HSA) and in micelles of sodium dodecylsulfate ( SDS ) and hexadecyltrimethylammonium chloride ( CTAC ). Spectrophotometric measurements showed that the surfactants SDS and CTAC induce monomerization of I, although the latter less efficiently than the former. This effect is less pronounced in the presence of HSA. The strength of this effect is evaluated through dimerization constants, which are Kd = (5 ± 1) × 105 m−1 in SDS , (1.5 ± 0.5) × 106 M −1 in CTAC , and (1.8 ± 0.9) × 106 M −1 in HSA. Fluorescence experiments confirm that aggregation of I drops as the concentration of surfactant is raised. Triplet quantum yields also decreased upon aggregation and were Φ T = 0.59, 0.16, and < 0.01 in SDS , CTAC , and HSA, respectively. These results indicate that the affinity of I for the environment is not just due to ionic interactions; hydrophobic interactions play an equally important role.

scholarly journals Lysine residue 240 of human serum albumin is involved in high-affinity binding of bilirubin

1978 ◽  
Vol 171 (2) ◽  
pp. 453-459 ◽  
Author(s):  
C Jacobsen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Lysine Residue ◽  
Water Soluble ◽  
High Affinity ◽  
Coupling Reagent ◽  
Peptide Fraction ◽  
Short Period ◽  
High Affinity Site

Bilirubin can be coupled covalently to albumin by using water-soluble carbodi-imide as coupling reagent. The optimal specificity in the attachment of bilirubin to the high-affinity site on the albumin molecule was obtained by treating an albumin-bilirubin complex with carbodi-imide in low concentrations and for a short period. The product was reduced, carboxymethylated and digested with trypsin. By fractionation on Sephadex G-50 (superfine grade) a peptide fraction containing most of the bilirubin label was isolated. Further purification by paper chromatography gave one peptide, consisting of residues 240-258. The peptide containined a single lysine residue, 240, and had an intact disulphide bridge. The results indicate that bilirubin is bound to lysine residue 240 at its high-affinity site on human serum albumin.

Water-Soluble α,β-Unsaturated Aldehydes of Cigarette Smoke Induce Carbonylation of Human Serum Albumin

2010 ◽  
Vol 12 (3) ◽  
pp. 349-364 ◽  
Author(s):  
Graziano Colombo ◽  
Giancarlo Aldini ◽  
Marica Orioli ◽  
Daniela Giustarini ◽  
Rosalba Gornati ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Cigarette Smoke ◽  
Water Soluble ◽  
Unsaturated Aldehydes

Release of Warfarin from Human Serum Albumin by Water‐soluble CdSe Nanotetrapods

ChemPhysChem ◽  
2020 ◽  
Vol 21 (24) ◽  
pp. 2709-2714 ◽  
Author(s):  
Sucheta Banerjee ◽  
Tanuja Kistwal ◽  
Amritha Sajeevan ◽  
Anindya Datta
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Water Soluble

scholarly journals Biocompatible CdSe/ZnS quantum dot micelles for long-term cell imaging without alteration to the native structure of the blood plasma protein human serum albumin

RSC Advances ◽  
2017 ◽  
Vol 7 (5) ◽  
pp. 2392-2402 ◽  
Author(s):  
Shanmugavel Chinnathambi ◽  
Norhidayah Abu ◽  
Nobutaka Hanagata
Keyword(s):  
Human Serum Albumin ◽  
Quantum Dot ◽  
Serum Albumin ◽  
Blood Plasma ◽  
Human Serum ◽  
Biological Samples ◽  
Cell Imaging ◽  
Water Soluble ◽  
Native Structure

Water soluble super paramagnetic CdSe/ZnS QD micelles can be useful for long-term imaging of biological samples.

scholarly journals Development and Validation Molecular Docking Analysis of Human serum albumin (HSA)

2021 ◽  
Author(s):  
IVAN VITO FERRARI ◽  
Paolo Patrizio
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Affinity ◽  
Water Soluble ◽  
Inhibition Constant ◽  
Ligand Efficiency ◽  
Protein Preparation ◽  
Docking Analysis

Background: HAS (Human Serum Albumin) is a highly water-soluble globular plasma protein, with a relative molecular weight (g/mol) of 67 KDa, consisting of 585 amino acid residues. In this study, we have investigated the interaction of the crystal structures complexed in human serum albumin at resolutions of 2.8 to 2.0: Camptothecin, 9-amino-camptothecin, Etoposide, Teniposide, Bicalutamide and Idarubicin, using a bioinformatic approach, estimated by Pyrx Virtual Screen Tool and AMDock ( AMDock, Assisted Molecular Docking). We have analyzed a validated protocol, studying several parameters, as Binding Affinity, RMSD value, Ligand Efficiency, and Inhibition constant (Ki value). Methods: Human Serum Albumin protein preparation was characterized with several programs, as Chimera, MGLTools 1.5.6, Swiss PDB Viewer Software to perform docking analysis by Autodock Vina estimated with Pyrx Software. Results: In this work, we found crystalized camptothecin, 9-amino-camptothecin and teniposide, gave excellent results for Binding Affinity, (kcal/mol), RMSD value (A ), inhibition constant Ki value (nM): -Binding Affinity of 9-amino-camptothecin (ca.-10 kcal/mol), camptothecin ( -9 kcal/mol) and teniposide ( -11 kcal/mol, -RMSD Value of 9 -amino-camptothecin (ca.1.8 A ), camptothecin (ca.2.2 A ) and teniposide (ca. 3.6 A), - Ki Value: 9 -amino-camptothecin (ca 59 nM), camptothecin ( ca 183 nM) and teniposide ( ca 9 nM), -Ligand efficiency: of 9 -amino-camptothecin(ca -0.35 kcal/mol) , camptothecin (ca -0.34 kcal/mol) and teniposide (ca -0.24 kcal/mol Conclusions: We explored the best three crystallized ligand in Human Serum Albumin. Moreover, we have observed a complete overlap, during the re-docking analysis phase, estimated by chimera Software. Therefore we have concluded that ID PDB Crystal 4L8U human serum albumin-Crystallised 9 -amino Camptothecin; ID PDB Crystal 4L9K human serum albumin- Crystallised Camptothecin and ID PDB Crystal 4L9Q human serum albumin-Crystallised teniposide be used as a possible as a reference template protein to be compared with the target protein, by Docking molecular analysis.

scholarly journals A Deferasirox Derivative That Acts as a Multifaceted Platform for the Detection and Quantification of Fe3+

Chemosensors ◽  
2021 ◽  
Vol 9 (4) ◽  
pp. 68
Author(s):  
Axel Steinbrueck ◽  
Adam C. Sedgwick ◽  
Suh-Mi Hwang ◽  
Sajal Sen ◽  
Michael Y. Zhao ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Metal Cation ◽  
Iron Chelator ◽  
Water Soluble ◽  
Aqueous Samples ◽  
Colorimetric Chemosensor ◽  
Turn On ◽  
Detection And Quantification

Here, we report that ExSO3H, a synthetically accessible, water-soluble, non-toxic derivative of the clinical iron chelator deferasirox, acts as a colorimetric chemosensor that permits the detection and quantification of Fe3+ in aqueous samples at pH 2–5. In addition, we observed that a fluorescent turn-on response was produced when this chelator was allowed to interact with human serum albumin (HSA). This fluorescence was quenched in the presence of Fe3+, thus allowing us to monitor the presence of this biologically important metal cation via two independent methods.

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