Intramolecular Complex Formation of Poly(N-isopropylacrylamide) with Human Serum Albumin

2003 ◽  
Vol 4 (3) ◽  
pp. 728-735 ◽  
Author(s):  
Toshiyuki Matsudo ◽  
Kazuyoshi Ogawa ◽  
Etsuo Kokufuta
Keyword(s):  
Human Serum Albumin ◽  
Complex Formation ◽  
Serum Albumin ◽  
Human Serum ◽  
Intramolecular Complex

scholarly journals Human Serum Albumin-[Ru(Phen)3]2+ Complex Formation Studied by Optical Spectroscopies

2016 ◽  
Vol 110 (3) ◽  
pp. 48a ◽  
Author(s):  
Zuzana Jurasekova ◽  
Veronika Huntosova ◽  
Dominik Belej ◽  
Pavol Miskovsky ◽  
Daniel Jancura
Keyword(s):  
Human Serum Albumin ◽  
Complex Formation ◽  
Serum Albumin ◽  
Human Serum

scholarly journals Interaction of human serum albumin with short polyelectrolytes: a study by calorimetry and computer simulations

Soft Matter ◽  
2015 ◽  
Vol 11 (23) ◽  
pp. 4630-4639 ◽  
Author(s):  
Shun Yu ◽  
Xiao Xu ◽  
Cemil Yigit ◽  
Markus van der Giet ◽  
Walter Zidek ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Complex Formation ◽  
Serum Albumin ◽  
Human Serum ◽  
Computer Simulations ◽  
Salt Concentration ◽  
Polyelectrolyte Complex ◽  
P Protein ◽  
Simulation Results

Protein–polyelectrolyte complex formation was studied by combining experimental with simulation results. By varying salt concentration and temperature, our study reveals the importance of electrostatics and the release of counterions.

scholarly journals Fluorescence Enhancement Based Quantification of Human Serum Albumin from Biological Sample Using Indole Based Nanosuspension: Molecular Interactions and Molecular Docking Studies

2021 ◽  
Author(s):  
Sonali B. Suryawanshi ◽  
Netaji K. Desai ◽  
Anita J. Bodake ◽  
Shivajirao R. Patil
Keyword(s):  
Particle Size ◽  
Molecular Docking ◽  
Human Serum Albumin ◽  
Complex Formation ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Interactions ◽  
Biological Sample ◽  
Fluorescence Enhancement ◽  
Docking Studies

Abstract Fluorescent 3-[(E)-(2-phenylhydrazinylidene) methyl]-1H-indole (PHI) was synthesized by condensation of indole-3carboxaldehyde and phenyl hydrazine in presence of acetic acid and ethanol and after spectral characterization used further to prepare its aqueous nano suspension by reprecipitation method using polyvinylpyrrolidone (PVP) as stabilizer. The average particle size of nano suspension measured by Dynamic Light Scattering (DLS) was found 77.5 nm while FESEM microphotograph showed spherical morphology. The blue shift in the absorption spectrum and stokes shifted fluorescence of nanosuspension of PHI compared to its monomer spectrum in dilute solution indicate formation of H-type aggregate by face to face overlapping of the molecules.The aggregation induced enhanced emission (AIEE) of PVP capped nanosuspension of PHI is increased appreciably by presence of aqueous solution of human serum albumin (HSA). A suitable mechanism of molecular binding interactions based on complex formation between PHI nanoaggregate and HSA through PVP is proposed. Fluorescence life time, zeta potential and particle size data of PHI nanoparticles (PHINPs) obtained in presence of different amounts of HSA are in support of molecular interactions leading to complex formation. The molecular docking studies showed that HSA and PVP capped PHINPs exhibit strong hydrogen bonding interaction. The fluorescence enhancement effect induced in PHI nanosuspension is used further to develop analytical method for quantitative estimation of HSA in aqueous biological sample solution.

scholarly journals Comparative studies of the binding of some ligands to human serum albumin non-covalently attached to immobilized Cibacron Blue, or covalently immobilized on Sepharose, by column affinity chromatography

1983 ◽  
Vol 213 (2) ◽  
pp. 387-390 ◽  
Author(s):  
C Lagercrantz ◽  
T Larsson
Keyword(s):  
Fatty Acids ◽  
Salicylic Acid ◽  
Human Serum Albumin ◽  
Complex Formation ◽  
Ligand Binding ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Binding Strength ◽  
Cibacron Blue

A comparative study of the ligand-binding properties of human serum albumin was performed by the technique of affinity chromatography with the protein attached to immobilized Cibacron Blue F3GA (Blue Sepharose), or covalently immobilized on Sepharose. The binding strength of octanoate, decanoate and dodecanoate is much weaker when human serum albumin is attached to immobilized Cibacron Blue, indicating that the binding sites for fatty acids are involved in the attachment of human serum albumin to immobilized Cibacron Blue. The results revealed additional alterations of the ligand binding when human serum albumin was attached to immobilized Cibacron Blue, involving sites outside of the binding domains of fatty acids. Thus the stereoselective binding of L-tryptophan was abolished, and the resolution of the warfarin enantiomers was impaired. However, the binding strength of warfarin and salicylic acid was rather close to the values observed with human serum albumin covalently immobilized on Sepharose. It is suggested that the availability of the binding sites for L-tryptophan, warfarin and salicylic acid is partially blocked by the complex between albumin and the dye without direct participation in the complex-formation. An alternative interpretation involves an allosteric mechanism brought about by complex-formation between serum albumin and the immobilized Cibacron Blue.

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