Effect of Ionic Liquids on the Solution Structure of Human Serum Albumin

2011 ◽  
Vol 12 (4) ◽  
pp. 1072-1079 ◽  
Author(s):  
Yasar Akdogan ◽  
Matthias J. N. Junk ◽  
Dariush Hinderberger
Keyword(s):  
Ionic Liquids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Solution Structure

scholarly journals Characterization of the Solution Structure of Human Serum Albumin Loaded with a Metal Porphyrin and Fatty Acids

2011 ◽  
Vol 100 (9) ◽  
pp. 2293-2301 ◽  
Author(s):  
Matthias J.N. Junk ◽  
Hans W. Spiess ◽  
Dariush Hinderberger
Keyword(s):  
Fatty Acids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Solution Structure ◽  
Metal Porphyrin

Effect of ketoprofen-based ionic liquids on secondary structure and thermal stability of human serum albumin

2020 ◽  
Vol 142 (5) ◽  
pp. 1911-1917
Author(s):  
Proletina Kardaleva ◽  
Maya Guncheva ◽  
Svetla Todinova ◽  
Ivan Angelov ◽  
Paula Ossowicz ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Ionic Liquids ◽  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Thermal Stability Of

Selective binding and dynamics of imidazole alkyl sulfate ionic liquids with human serum albumin and collagen – a detailed NMR investigation

2018 ◽  
Vol 20 (14) ◽  
pp. 9256-9268 ◽  
Author(s):  
R. Ravikanth Reddy ◽  
Ganesh Shanmugam ◽  
Balaraman Madhan ◽  
B. V. N. Phani Kumar
Keyword(s):  
Ionic Liquids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Spin Relaxation ◽  
Alkyl Sulfate ◽  
Binding Affinities ◽  
Selective Binding ◽  
Std Nmr ◽  
Anionic Part

STD NMR and selective spin-relaxation analysis evidenced the selective binding (anionic part) of imidazole alkyl sulfate ionic liquids with proteins (HSA and collagen). These studies also enabled the ionic liquids to be ranked based on their binding affinities with the proteins of study.

The effects of poly(ethylene glycol) on the solution structure of human serum albumin

Biopolymers ◽  
2005 ◽  
Vol 78 (5) ◽  
pp. 231-236 ◽  
Author(s):  
C. Ragi ◽  
M. R. Sedaghat-Herati ◽  
A. Ahmed Ouameur ◽  
H. A. Tajmir-Riahi
Keyword(s):  
Human Serum Albumin ◽  
Ethylene Glycol ◽  
Serum Albumin ◽  
Human Serum ◽  
Solution Structure ◽  
Poly Ethylene Glycol ◽  
Poly Ethylene

Behavior of Acrylodan-Labeled Human Serum Albumin Dissolved in Ionic Liquids

2008 ◽  
Vol 47 (3) ◽  
pp. 560-569 ◽  
Author(s):  
Taylor A. McCarty ◽  
Phillip M. Page ◽  
Gary A. Baker ◽  
Frank V. Bright
Keyword(s):  
Ionic Liquids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum

Dynamics of Loop 1 of Domain I in Human Serum Albumin When Dissolved in Ionic Liquids

2009 ◽  
Vol 113 (38) ◽  
pp. 12825-12830 ◽  
Author(s):  
Taylor A. Page ◽  
Nadine D. Kraut ◽  
Phillip M. Page ◽  
Gary A. Baker ◽  
Frank V. Bright
Keyword(s):  
Ionic Liquids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Domain I

scholarly journals Interaction of ionic liquids with human serum albumin in the view of bioconcentration: a preliminary study

2022 ◽  
Author(s):  
Dorota Kowalska ◽  
Stefan Stolte ◽  
Dariusz Wyrzykowski ◽  
Piotr Stepnowski ◽  
Joanna Dołżonek
Keyword(s):  
Ionic Liquids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Chemical Compounds ◽  
Blood Proteins ◽  
Binding Properties ◽  
Imidazolium Cations ◽  
Preliminary Study ◽  
Anion Interaction

AbstractBioaccumulation potential is critical in PBT and risk assessment of chemicals. However, for ionic liquids (ILs), this aspect remains neglected. It is especially important to fill this gap, because for this group of compounds, existing data confirm their risk of being environmentally persistent and toxicity. Moreover, considering preliminary reports on the interactions of ILs with lipids, it may be assumed that ILs have a higher potential for bioaccumulation than indicated by previous estimations built upon octanol–water partition coefficients. Moreover, the bioconcentration of ionizable chemical compounds may also be strongly related to plasma protein contents. Therefore, in this work, the affinity of a set of imidazolium cations and organic anions, and their combination to human serum albumin (HSA) was determined. The obtained results reveal that both cations and anions can be strongly bound to HSA, and blood proteins might play an important role in overall bioaccumulation. Furthermore, it was observed that HSA binding properties towards IL cations depend on the hydrophobicity of cations. The obtained data also provide indication that cation–anion interaction may affect ILs ions affinity to HSA.

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