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
2011 ◽  
Vol 12 (4) ◽  
pp. 1072-1079 ◽  
Author(s):  
Yasar Akdogan ◽  
Matthias J. N. Junk ◽  
Dariush Hinderberger

2020 ◽  
Vol 142 (5) ◽  
pp. 1911-1917
Author(s):  
Proletina Kardaleva ◽  
Maya Guncheva ◽  
Svetla Todinova ◽  
Ivan Angelov ◽  
Paula Ossowicz ◽  
...  

2018 ◽  
Vol 20 (14) ◽  
pp. 9256-9268 ◽  
Author(s):  
R. Ravikanth Reddy ◽  
Ganesh Shanmugam ◽  
Balaraman Madhan ◽  
B. V. N. Phani Kumar

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.


2022 ◽  
Author(s):  
Dorota Kowalska ◽  
Stefan Stolte ◽  
Dariusz Wyrzykowski ◽  
Piotr Stepnowski ◽  
Joanna Dołżonek

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.


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

2017 ◽  
Vol 40 (10) ◽  
pp. 1813-1817 ◽  
Author(s):  
Sadaharu Matsushita ◽  
Koji Nishi ◽  
Yasunori Iwao ◽  
Yu Ishima ◽  
Hiroshi Watanabe ◽  
...  

PLoS ONE ◽  
2020 ◽  
Vol 15 (10) ◽  
pp. e0240580
Author(s):  
Martina Steglich ◽  
Rodrigo Lombide ◽  
Ignacio López ◽  
Madelón Portela ◽  
Martín Fló ◽  
...  

2016 ◽  
Vol 27 (10) ◽  
pp. 2271-2275 ◽  
Author(s):  
James T. Patterson ◽  
Henry D. Wilson ◽  
Shigehiro Asano ◽  
Napon Nilchan ◽  
Roberta P. Fuller ◽  
...  

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