Comparison of the Thermal Denaturing of Human Serum Albumin in the Presence of Guanidine Hydrochloride and 1-Butyl-3-methylimidazolium Ionic Liquids

2013 ◽  
Vol 117 (8) ◽  
pp. 2378-2383 ◽  
Author(s):  
William T. Heller
Keyword(s):  
Ionic Liquids ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Guanidine Hydrochloride

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

At very low concentrations known chaotropes act as kosmotropes for the N and B isoforms of human serum albumin

2013 ◽  
Vol 91 (2) ◽  
pp. 72-78 ◽  
Author(s):  
Priyankar Sen ◽  
Mohd Moin Khan ◽  
Asif Equbal ◽  
Ejaz Ahmad ◽  
Rizwan Hasan Khan
Keyword(s):  
Protein Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Electrostatic Interaction ◽  
Tertiary Structure ◽  
Guanidine Hydrochloride ◽  
Micelle Formation ◽  
Low Concentrations ◽  
Secondary And Tertiary Structure

Very few studies have been done to understand the effect of millimolar concentrations of chaotropes on protein structure. In our previous study we observed that the secondary and tertiary structure of human serum albumin (HSA) increases in the presence of 5 mmol/L urea. Micelle formation in amphoteric detergents increases in the presence of equivalent concentrations of urea. Here, we observed a significant increase in the secondary and tertiary structure of HSA. Interestingly, guanidine hydrochloride, another chaotropic agent, also shows a similar effect. Our results show electrostatic interaction may play a role in neutral to basic transition in HSA. This study further supports the claim that at millimolar concentrations the chaotropes may act as kosmotropes for proteins.

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

scholarly journals Role of Arg-410 and Tyr-411 in human serum albumin for ligand binding and esterase-like activity

2000 ◽  
Vol 349 (3) ◽  
pp. 813-819 ◽  
Author(s):  
Hiroshi WATANABE ◽  
Sumio TANASE ◽  
Keisuke NAKAJOU ◽  
Toru MARUYAMA ◽  
Ulrich KRAGH-HANSEN ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Ligand Binding ◽  
Serum Albumin ◽  
Human Serum ◽  
Aromatic Ring ◽  
Recombinant Proteins ◽  
Expression System ◽  
Guanidine Hydrochloride ◽  
Enzymic Activity ◽  
Phenolic Oxygen

Recombinant wild-type human serum albumin (rHSA), the single-residue mutants R410A, Y411A, Y411S and Y411F and the double mutant R410A/Y411A were produced using a yeast expression system. The recombinant proteins were correctly folded, as they had the same stability towards guanidine hydrochloride and the same CD spectrum as HSA isolated from serum (native HSA). Thus the global structures of the recombinant proteins are probably very similar to that of native HSA. We investigated, by ultrafiltration and CD, the high-affinity binding of two representative site II ligands, namely ketoprofen and diazepam. According to the crystal structure of HSA, the residues Arg-410 and Tyr-411 protrude into the centre of site II (in subdomain 3A), and the binding results showed that the guanidino moiety of Arg-410, the phenolic oxygen and the aromatic ring of Tyr-411 are important for ketoprofen binding. The guanidino moiety probably interacts electrostatically with the carboxy group of ketoprofen, the phenolic oxygen could make a hydrogen-bond with the keto group of the ligand, and the aromatic ring may participate in a specific stacking interaction with one of or both of the aromatic rings of ketoprofen. By contrast, Arg-410 is not important for diazepam binding. The two parts of Tyr-411 interact favourably with diazepam, and probably do so in the same way as with ketoprofen. In addition to its unique ligand binding properties, HSA also possesses an esterase-like activity, and studies with p-nitrophenyl acetate as a substrate showed that, although Arg-410 is important, the enzymic activity of HSA is much more dependent on the presence of Tyr-411. A minor activity could be registered when serine, but not alanine or phenylalanine, was present at position 411.

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.

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.

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
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