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

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.

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 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.

Different rates of formation of secondary and tertiary structure during renaturation of urea-denatured human serum albumin

1989 ◽  
Vol 54 (9) ◽  
pp. 2542-2549 ◽  
Author(s):  
Josef Chmelík
Keyword(s):  
Protein Folding ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Disulfide Bonds ◽  
Tertiary Structure ◽  
Hydrophobic Interactions ◽  
Protein Structures ◽  
Three Dimensional ◽  
Comparison Of The Results

A comparison of the results of our polarimetric measurements with the polarographic experiments reported earlier shows that the restoration of the secondary structure during the renaturation of human serum albumin is a process which is faster than the formation of the tertiary structure. These results, which are in agreement with the data on the kinetic control of protein folding, are discussed from the viewpoint of the importance of the individual types of interactions which take place during the formation and stabilization of three-dimensional protein structures. We have been able to demonstrate the great importance of electrostatic and hydrophobic interactions which together with the disulfide bonds are essential for the reversibility of the denaturation phenomena. The discussion also shows the essential role which evolution processes play in the selection of the mode of protein folding.

scholarly journals Spectroscopic Technique-Based Comparative Investigation on the Interaction of Theaflavins with Native and Glycated Human Serum Albumin

Molecules ◽  
2019 ◽  
Vol 24 (17) ◽  
pp. 3171 ◽  
Author(s):  
Jinhui Xu ◽  
Mengyuan Wang ◽  
Yizhe Zheng ◽  
Lin Tang
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Three Dimensional ◽  
Black Tea ◽  
Comparative Investigation ◽  
Spectroscopic Technique ◽  
Serum Albumins ◽  
Hydrophobic Force ◽  
Site Competition

Theaflavin is a kind of multi-pharmacological and health beneficial black tea factor. The aim of this study is to investigate the mechanisms by which theaflavin interacts with glycosylated and non-glycosylated serum albumins and compares their binding properties. Fluorescence and ultraviolet spectra indicated that theaflavin interacted with native and glycated human serum albumin through a static quenching mechanism and had a higher degree of quenching of human serum albumin. The thermodynamic parameters revealed that the combinations of theaflavin with native and glycated human serum albumin were a spontaneous endothermic reaction, and the hydrophobic force was a major driving force in the interaction process. Zeta potential, particle size, synchronous fluorescence, three-dimensional fluorescence spectroscopy and circular dichroism further clarified the effect of theaflavin on the conformation of human serum albumin structure were more pronounced. In addition, site competition experiments and molecular docking technique confirmed that the binding sites of theaflavin on both native and glycated human serum albumin were bound at site II. This study had investigated the effects of glycation on the binding of HSA with polyphenols and the potential nutriology significance of these effects.

Sign in / Sign up

Export Citation Format

Share Document