Chiroptical Properties of Bilirubin-Serum Albumin Binding Sites

Chirality ◽  
2013 ◽  
Vol 25 (4) ◽  
pp. 257-263 ◽  
Author(s):  
Iryna Goncharova ◽  
Sergey Orlov ◽  
Marie Urbanová
Keyword(s):  
Serum Albumin ◽  
Binding Sites ◽  
Albumin Binding ◽  
Chiroptical Properties

scholarly journals Candida albicans exhibit two classes of cell surface binding sites for serum albumin defined by their affinity, abundance and prospective role in interkingdom signalling

PLoS ONE ◽  
2021 ◽  
Vol 16 (7) ◽  
pp. e0254593
Author(s):  
Claire Teevan-Hanman ◽  
Paul O’Shea
Keyword(s):  
Candida Albicans ◽  
Cell Surface ◽  
Serum Albumin ◽  
Yeast Cell ◽  
Binding Sites ◽  
Culture Media ◽  
Affinity Binding ◽  
Albumin Binding ◽  
Spectroscopic Techniques ◽  
Surface Binding

Serum albumin binding to the yeast form of Candida albicans is described. Two populations of binding site are identified using two complementary spectroscopic techniques: an extrinsic fluorescent probe, 3-hexa-decanoyl-7-hydrocoumarin ([HEXCO) added to the C. albicans yeast cell surface that records the electrostatic surface potential and so responds to the surface binding of serum albumin and secondly a light scattering technique that reveals how albumin modulates aggregation of the yeast population. The albumin binding sites are found to possess different binding affinities and relative abundance leading to different total binding capacities. These are characterized as a receptor population with high affinity binding (Kd ~ 17 μM) but relatively low abundance and a separate population with high abundance but much lower affinity (Kd ~ 364 μM). The low-affinity binding sites are shown to be associated with the yeast cell aggregation. These values are found be dependent on the C. albicans strain and the nature of the culture media; some examples of these effects are explored. The possible physiological consequences of the presence of these sites are speculated in terms of evading the host’s immune response, biofilm formation and possible interkingdom signaling processes.

Exploration of human serum albumin binding sites by docking and molecular dynamics flexible ligand–protein interactions

Biopolymers ◽  
2010 ◽  
Vol 93 (2) ◽  
pp. 161-170 ◽  
Author(s):  
Omar Deeb ◽  
Martha Cecilia Rosales-Hernández ◽  
Carlos Gómez-Castro ◽  
Ramón Garduño-Juárez ◽  
José Correa-Basurto
Keyword(s):  
Molecular Dynamics ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Protein Interactions ◽  
Binding Sites ◽  
Albumin Binding ◽  
Human Serum Albumin Binding

A molecular dynamics study of human serum albumin binding sites

Il Farmaco ◽  
2005 ◽  
Vol 60 (6-7) ◽  
pp. 485-495 ◽  
Author(s):  
Roberto Artali ◽  
Gabriella Bombieri ◽  
Luisella Calabi ◽  
Antonio Del Pra
Keyword(s):  
Molecular Dynamics ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Sites ◽  
Albumin Binding ◽  
Human Serum Albumin Binding

Conformational properties of serum albumin binding sites in rats with different behaviour in the open field test

Stress ◽  
2006 ◽  
Vol 9 (1) ◽  
pp. 53-60 ◽  
Author(s):  
Yu. A. Gryzunov ◽  
E. V. Koplik ◽  
N. V. Smolina ◽  
L. B. Kopaeva ◽  
G. E. Dobretsov ◽  
...  
Keyword(s):  
Serum Albumin ◽  
Open Field ◽  
Field Test ◽  
Binding Sites ◽  
Open Field Test ◽  
Albumin Binding ◽  
Conformational Properties

The serum albumin-binding region of streptococcal protein G: a bacterial fusion partner with carrier-related properties

1997 ◽  
Vol 201 (1) ◽  
pp. 115-123 ◽  
Author(s):  
Anders Sjölander ◽  
Per-Åke Nygren ◽  
Stefan Ståhl ◽  
Klavs Berzins ◽  
Mathias Uhlén ◽  
...  
Keyword(s):  
Serum Albumin ◽  
Protein G ◽  
Albumin Binding ◽  
Fusion Partner ◽  
Binding Region ◽  
Streptococcal Protein G
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