The binding constant for amyloid Aβ40 peptide interaction with human serum albumin

2007 ◽  
Vol 364 (3) ◽  
pp. 714-718 ◽  
Author(s):  
Małgorzata Rózga ◽  
Marcin Kłoniecki ◽  
Agnieszka Jabłonowska ◽  
Michał Dadlez ◽  
Wojciech Bal
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Constant ◽  
Peptide Interaction

scholarly journals Interaction of Warfarin with Human Serum Albumin and Effect of Ferulic Acid on the Binding

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
Qiang Li ◽  
Wen-yue Yang ◽  
Ling-ling Qu ◽  
Huan-Yang Qi ◽  
Yun Huang ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Ferulic Acid ◽  
Human Serum ◽  
Binding Constant ◽  
Oral Anticoagulant ◽  
Combined Treatment ◽  
Hill Coefficient ◽  
Free Concentration ◽  
Risk Of Bleeding

Angelica sinensis(Oliv.) Diels combined treatment with warfarin would increase the risk of bleeding. Ferulic acid is an abundant hydroxycinnamic acid inA. sinensisand warfarin is the most widely used oral anticoagulant. The studies on supermolecular interaction of warfarin with human serum albumin (HSA) and the influence of ferulic acid on the binding would contribute to the understanding of the metabolic processes of warfarin and the effect of ferulic acid. We focus on investigating the effect of warfarin on fluorescence spectrum of human serum albumin (HSA), fluorescence quenching mechanism, binding constant, Hill coefficient, binding mode, and the effect of different ferulic acid concentrations on the binding. Warfarin quenched the intrinsic fluorescence of HSA mainly by static quenching. Accession of ferulic acid reduced the binding of HSA-warfarin. By decreasing binding constant and the Hill coefficient of warfarin with HSA, ferulic acid could improve the plasma concentration of free warfarin, which would increase the risk of bleeding. Warfarin’s free concentration increased at least 50% under the condition of simulated human body. The results indicated thatA. sinensiscombined treatment with warfarin would increase the risk of bleeding. And the results provide an important theoretical support for warfarin used as oral anticoagulant.

scholarly journals Reaction of the Anticancer Organometallic Ruthenium Compound, [(η6-p-Cymene)Ru(ATSC)Cl]PF6 with Human Serum Albumin

2010 ◽  
Vol 2010 ◽  
pp. 1-7 ◽  
Author(s):  
Floyd A. Beckford
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Thermodynamic Analysis ◽  
Binding Constant ◽  
Enthalpy Of Reaction ◽  
Infrared Spectrophotometry ◽  
Ruthenium Compound ◽  
Different Temperatures ◽  
Entropy Of Reaction

The reaction of [(η6-p-cymene)Ru(ATSC)Cl]PF6 (ATSC =9-anthraldehyde thiosemicarbazone) with human serum albumin was investigated at different temperatures using fluorescence and infrared spectrophotometry. The binding constant, K, for the reaction was determined using a number of different methods. Using a modified Stern-Volmer equation, K was determined to be 9.09×104,12.1×104, and 13.1×104 M−1 at 293 K, 298 K, and 308 K, respectively. A thermodynamic analysis showed that the reaction is spontaneous with ΔG being negative. The enthalpy of reaction ΔH=16.5 kJ mol−1 and the entropy of reaction ΔS=152 Jmol−1K−1. The values of ΔH and ΔS suggest that hydrophobic forces are dominant in the mode of interaction and that the process is mostly entropy driven.

scholarly journals BINDING STUDIES OF VALGANCICLOVIR TO HUMAN SERUM ALBUMIN BY MULTISPECTROSCOPIC TECHNIQUES

2018 ◽  
Vol 10 (10) ◽  
pp. 87
Author(s):  
Lade Somaji ◽  
Ravi Rapolu
Keyword(s):  
Molecular Modeling ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Conformational Changes ◽  
Binding Constant ◽  
Electrostatic Interactions ◽  
Hydrophobic Interactions ◽  
Experimental Studies ◽  
Binding Studies

Objective: The aim of the present study was to investigate the mode and mechanism of interactions involved towards binding of valganciclovir (VGC) with Human Serum Albumin (HSA) by spectroscopic and molecular modeling studies which can be extrapolated for the ten folds increase of bioavailability over its prodrug galanciclovir.Methods: Herein we employed fluorescence spectroscopy for evaluating the binding constant value, site of interaction and changes in the microenvironment of HSA fluorophores. Circular dichroism (CD) and UV-Visible spectroscopy is used for conformational changes of HSA in the event of binding of valaganciclovir. These experimental studies were further corroborated with molecular modeling studies.Results: Considerable quenching of fluorescence intensities of fluorophores in the presence of VGC showed that VGC interacts with HSA strongly with a binding constant of 4.11x104 M-1 with a free energy change of-6.26 Kcal/mol. Synchronous fluorescence and CD studies show that the microenvironment and confirmation of HSA are slightly altered in the presence of VGC. Though site marker experiments does not give any clue for identification of site, molecular docking studies showed that VGC binds to site IB of HSA.Conclusion: The weaker dominant electrostatic interactions with minor contributions of hydrophobic interactions of VGC with HSA at site IB (catalytic domain) might be the probable reason for the relative increase of hydrolysis of VGC to galanciclovir. And moderate binding constant value with HSA implies that HSA can be able to transport VGC under physiological conditions. 

scholarly journals Binding of porphyrin to human serum albumin. Structure–activity relationships

1990 ◽  
Vol 270 (2) ◽  
pp. 325-330 ◽  
Author(s):  
S Cohen ◽  
R Margalit
Keyword(s):  
Photodynamic Therapy ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Protein Binding ◽  
Human Serum ◽  
Binding Sites ◽  
Binding Constant ◽  
Drug Carrier ◽  
Haematoporphyrin Derivative ◽  
Binding Studies

The equilibrium binding of hydroxyethyl vinyl deuteroporphyrin (HVD) and of irreversible porphyrin aggregates to human serum albumin was studied at the molecular level. This protein may function as an endogenous drug carrier for porphyrins in photodynamic therapy of tumours. HVD-protein binding studies revealed two types of binding sites, which are attributed to the two HVD isomers. The binding constant for the high-affinity isomer, 2.1 (+/- 0.3) x 10(8) M-1, is similar to that previously determined for protoporphyrin. At the same time the binding constant for the lower-affinity HVD isomer, 1.8(+/- 0.3) x 10(6) M-1, is similar to that previously determined for haematoporphyrin. Irreversible porphyrin aggregates were purified from the haematoporphyrin derivative and from Photofrin and are defined by spectral and chromatographic data. Gel-exclusion studies indicate that the dominant size of these aggregates is ten porphyrin monomeric units. The protein-binding constant of these aggregates is 1.7(+/- 0.2) x 10(5) M-1, with four binding sites per protein molecule. The distinction between the HVD isomers along the porphyrin-protein affinity sequence gives insight into the relationship of porphyrin structure to porphyrin-albumin binding. On the basis of this study an evaluation of human serum albumin as an endogenous carrier for porphyrins (at various aggregation states) in photodynamic therapy of tumours is presented.

Sign in / Sign up

Export Citation Format

Share Document