4.4 Article

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

Journal

CHEMICAL PAPERS
Volume 76, Issue 4, Pages 2405-2417

Publisher

SPRINGER INT PUBL AG
DOI: 10.1007/s11696-021-02021-y

Keywords

Protein binding; Bioaccumulation; Bioconcentration; Ionic liquids; Human serum albumin

Funding

  1. Institutional Strategy of the University of Bremen - German Excellence Initiative
  2. Deutsche Forschungsgemeinschaft (DFG), German Research Foundation [380298548]
  3. National Science Centre (Poland) [NCN2016/23/G/ST5/04245]

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The bioaccumulation potential of ionic liquids (ILs) is often overlooked, despite their confirmed environmental persistence and toxicity risk. Studies have shown that ILs can strongly bind to human serum albumin (HSA), indicating a potential role of blood proteins in bioaccumulation. Additionally, the interaction between IL cations and anions may also affect their affinity to HSA.
Bioaccumulation 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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