scholarly journals Fluorescence study on the interaction of human serum albumin with loureirin B

2010 ◽  
Vol 24 (5) ◽  
pp. 547-557 ◽  
Author(s):  
Xu Chen ◽  
Jia-Ming Ma ◽  
Ke-Lan Yong ◽  
Jing-Ci Lv ◽  
Xia-Bing Zhang
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Spectra ◽  
Three Dimensional ◽  
Entropy Change ◽  
Enthalpy Change ◽  
Dynamic Quenching ◽  
Fluorescence Study ◽  
Loureirin B

The interaction between loureirin B (Lour B) and human serum albumin (HSA) was investigated by fluorescence and UV–vis absorption spectroscopy. Experimental results indicated that loureirin B had a strong ability to quench the intrinsic fluorescence of HSA through a dynamic quenching procedure. The fluorescence quenching data revealed that the quenching constants (KSV) 2.68×104, 3.30×104and 4.10×104l/mol at 300, 310 and 320 K, respectively. Based on the thermodynamic parameters obtained, the positive values of enthalpy change ΔH and entropy change ΔS suggested that hydrophobic forces played a major role in the interaction of Lour B with HSA. According to Förster theory of energy transfer, the distancerbetween HSA and Lour B was calculated to be 2.85 nm. Furthermore, the effect of Lour B on the conformation of HSA was analyzed by synchronous fluorescence and three-dimensional fluorescence spectra.

scholarly journals The interaction between protocatechuic aldehyde and human serum albumin using three-dimensional fluorescence techniques

2011 ◽  
Vol 26 (3) ◽  
pp. 195-201 ◽  
Author(s):  
Jing Tian ◽  
Changyun Chen ◽  
Mengwei Xue
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Spectra ◽  
Three Dimensional ◽  
Entropy Change ◽  
Tryptophan Residue ◽  
Standard Entropy ◽  
Protocatechuic Aldehyde

The binding mechanism between protocatechuic aldehyde (PA) and human serum albumin (HSA) was investigated by fluorescence spectroscopy at different temperatures. It is proved that the fluorescence quenching of HSA by PA is not results of the formation of PA–HSA complex. The equilibrium constantKand the number of binding sitesnwere measured at different temperature by fluorescence quenching method. The standard enthalpy change (ΔH) and the standard entropy change (ΔS) of this interaction process were calculated to be 114.02 kJ · mol−1, 541.92 J · mol−1·K−1, respectively. According to the interaction between PA and HSA of thermodynamic parameters ΔHand ΔS, the major acting force can be measured. The synchronous fluorescence spectra shows the microenvironment of tryptophan residue is changed and the hydrophobicity is increased. Through three-dimensional (3D) fluorescence spectra can get some valuable structure changing information.

scholarly journals Three-dimensional structure of human serum albumin

Science ◽  
1989 ◽  
Vol 244 (4909) ◽  
pp. 1195-1198 ◽  
Author(s):  
D. Carter ◽  
X. He ◽  
S. Munson ◽  
P. Twigg ◽  
K. Gernert ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Three Dimensional Structure

Influence of Human Serum Albumin Glycation on the Binding Affinities for Natural Flavonoids

2019 ◽  
Vol 17 (1) ◽  
pp. 806-812
Author(s):  
Liangliang Liu ◽  
Yi Liu ◽  
Aiping Xiao ◽  
Shiyong Mei ◽  
Yixi Xie
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Small Molecules ◽  
Human Body ◽  
Binding Sites ◽  
Plasma Proteins ◽  
Fluorescence Spectra ◽  
Binding Affinities ◽  
Dietary Flavonoids

AbstractIncreasing the degree of glycation in diabetes could affect the ability of plasma proteins in binding to small molecules and active compounds. In this study, the influence of glycation of Human serum albumin (HSA) on the binding affinities for six dietary flavonoids was investigated by fluorescence spectra. Glycated HSA was prepared through incubation with glucose and characterized by several methods to confirm the glycation. It was found that the level of glycation increased with the increasing incubation time. The glycation of HSA increased the binding affinities for flavonoids by 1.40 to 48.42 times, which indicates that modifications caused by the glycation may have different influences on the interactions of flavonoids with HSA at separate binding sites on this protein. These results are valuable for understanding the influence of diabetes on the metabolism of flavonoids and other bioactive small molecules in human body.

Paclitaxel-induced formation of 3D nanocrystal superlattices within injectable protein-based hybrid nanoparticles

2018 ◽  
Vol 54 (82) ◽  
pp. 11586-11589
Author(s):  
Jeong Yu Lee ◽  
Ho Yeon Son ◽  
Jae Chul Park ◽  
Jongnam Park ◽  
Yoon Sung Nam
Keyword(s):  
Polyethylene Glycol ◽  
Iron Oxide ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Self Assembly ◽  
Three Dimensional ◽  
Superparamagnetic Iron Oxide ◽  
Hybrid Nanoparticles ◽  
Nanocrystal Superlattices

Self-assembly of monodisperse superparamagnetic iron oxide nanocrystals into a close-packed, three-dimensional (3D) superlattice is designed within cross-linked protein-based nanoparticles composed of human serum albumin and polyethylene glycol.

Fluorescence study of nile red bound to human serum albumin in buffer, denaturant, and reverse micelles

1995 ◽  
Author(s):  
Daniel M. Davis ◽  
David J. S. Birch ◽  
P. R. Gellert ◽  
Rodney S. Kittlety ◽  
Ronald M. Swart
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Reverse Micelles ◽  
Nile Red ◽  
Fluorescence Study

Comparison of three methods for analyzing loureirin B and human serum albumin interaction using capillary electrophoresis

2017 ◽  
Vol 38 (7) ◽  
pp. 1038-1043 ◽  
Author(s):  
Yuelin Zhang ◽  
Yijie Sha ◽  
Kai Qian ◽  
Xu Chen ◽  
Qin Chen
Keyword(s):  
Capillary Electrophoresis ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Loureirin B

scholarly journals Monitoring human serum albumin cell cultures using surface plasmon resonance (SPR) spectroscopy

2015 ◽  
Vol 4 (1) ◽  
pp. 77-83 ◽  
Author(s):  
A. Henseleit ◽  
C. Pohl ◽  
Th. Bley ◽  
E. Boschke
Keyword(s):  
Surface Plasmon Resonance ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Surface Plasmon ◽  
Cell Cultures ◽  
Plasmon Resonance ◽  
Incident Light ◽  
Three Dimensional ◽  
Critical Parameters

Abstract. Continuously monitoring cell cultures is essential for both controlling critical parameters and improving understanding of key processes. An ideal technique in this context is surface plasmon resonance (SPR) spectroscopy, which essentially exploits changes in the angle of incident light that occur when molecules bind to a surface. It provides the ability to monitor real-time changes in small concentrations of various molecules, with no need for additional labels or sample preparation. Here we present an SPR-based immunoassay for monitoring concentrations of human serum albumin (HSA), and compare its sensitivity when used in conjunction with a Biacore platform and the cheaper, smaller liSPR system. In conjunction with either system, the immunoassay can detect HSA (a hepatocyte viability marker) at concentrations typically present in three-dimensional hepatocyte cultures mimicking the liver used to evaluate effects of drug candidates before exposure to humans or animals. Furthermore, in conjunction with the liSPR system, it is sufficiently sensitive to measure the much lower HSA levels present in skin–hepatocyte co-cultures.

Sign in / Sign up

Export Citation Format

Share Document