Spectroscopic, Zeta-potential and Surface Plasmon Resonance analysis of interaction between potential anti-HIV tannins with different flexibility and human serum albumin

2020 ◽  
Vol 194 ◽  
pp. 111175
Author(s):  
Szymon Sekowski ◽  
Ewa Olchowik-Grabarek ◽  
Weronika Wieckowska ◽  
Artem Veiko ◽  
Lukasz Oldak ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Human Serum Albumin ◽  
Zeta Potential ◽  
Serum Albumin ◽  
Human Serum ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Surface Plasmon Resonance Analysis ◽  
Resonance Analysis ◽  
Anti Hiv

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.

scholarly journals Biomolecular Interaction Study of Cyclolinopeptide A with Human Serum Albumin

2010 ◽  
Vol 2010 ◽  
pp. 1-8 ◽  
Author(s):  
Ben Rempel ◽  
Bo Gui ◽  
Jason Maley ◽  
Martin Reaney ◽  
Ramaswami Sammynaiken
Keyword(s):  
Surface Plasmon Resonance ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Tertiary Structure ◽  
Temperature Sensitive ◽  
Interaction Study ◽  
Biomolecular Interaction

The kinetics, energetics, and structure of Cyclolinopeptide A binding with Human Serum Albumin were investigated with surface plasmon resonance and circular dichroism. The complex is formed through slow recognition kinetics that is temperature sensitive in the range of 20°C–37°C. The overall reaction was observed to be endothermic (ΔH=204 kJmol−1) and entropy driven (ΔS=746 Jmol−1K−1) with overall small changes to the tertiary structure.

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