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.

Cigarette smoke induces alterations in the drug-binding properties of human serum albumin

2014 ◽  
Vol 52 (4) ◽  
pp. 166-174 ◽  
Author(s):  
Marco Clerici ◽  
Graziano Colombo ◽  
Francesco Secundo ◽  
Nicoletta Gagliano ◽  
Roberto Colombo ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Cigarette Smoke ◽  
Drug Binding ◽  
Binding Properties

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 Combined spectroscopy methods and molecular simulations for the binding properties of trametinib to human serum albumin

RSC Advances ◽  
2018 ◽  
Vol 8 (9) ◽  
pp. 4742-4749 ◽  
Author(s):  
Zili Suo ◽  
Qiaomei Sun ◽  
Hongqin Yang ◽  
Peixiao Tang ◽  
Ruixue Gan ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Molecular Simulations ◽  
Binding Properties

Probing the binding properties of trametinib to human serum albumin.

scholarly journals 1723. Human Serum Albumin Regulates the Growth of Candida auris in vitro

2019 ◽  
Vol 6 (Supplement_2) ◽  
pp. S631-S632
Author(s):  
Jun Sakai
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Candida Species ◽  
Blood Protein ◽  
Albumin Concentration ◽  
Blood Proteins ◽  
Candida Auris ◽  
Xtt Assay ◽  
High Albumin

Abstract Background Candida auris is commonly detected in human ear secretions. However, C. auris occasionally causes bloodstream infections even in immunocompetent patients resulting in poor prognosis. It was speculated that C. auris growth within the blood might be regulated by proteins in the bloodstream. Thus, in this study, the potential role of blood proteins in the regulation of C. auris growth was investigated. Methods Five Candida species (C. albicans, C. auris, C. glabrata, C. parapsilosis, and C. tropicalis) were incubated overnight. Colony suspensions for each species were prepared and adjusted to OD 1.0 at absorbance 0.1. Then, human serum albumin (HSA) and bovine serum albumin (BSA) were diluted (2.5 g/dL–0.002 g/dL) and mixed with the suspensions. Mixed samples were adjusted to 100 μL and incubated on MHA plates at 35°C for 2 days. Then, 50 μL of the combined sample was extracted and streaked onto Yeast extract-Peptone-Dextrose (YPD) agar. The remaining 50 μL sample was analyzed using an XTT assay. Further testing was then conducted on the effects of a specific blood protein albumin on Candida. Thereby, C. albicans and C. auris were cultured following the procedure above and stained with Annexin V and PI. Results The growth of C. auris mixed with a high albumin concentration (2.5~0.15 g/dL) was regulated compared with that of other Candida species (P < 0.01) (Figures 1 and 2); however, the growth of C. auris mixed with a lower albumin concentration was similar to that of other species. The wash-out study showed that C. auris growth and survival in the high albumin concentration was not different than that of other species. Conclusion HSA and BSA regulated C. auris growth which led to increased necrosis of C. auris. Conversely, growth of the other Candida species was not regulated. Therefore, albumin might be involved in the growth and necrosis of C. auris. As the highest concentration at which albumin regulated C. auris growth was similar to that found in human serum, it is possible that serum albumin might help prevent C. auris from entering the bloodstream via the ear or skin. Disclosures All authors: No reported disclosures.

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