Perfluoroalkane sulfonyl fluorides non-covalently bind to human serum albumin at Sudlow's sites. (February 2019)
- Record Type:
- Journal Article
- Title:
- Perfluoroalkane sulfonyl fluorides non-covalently bind to human serum albumin at Sudlow's sites. (February 2019)
- Main Title:
- Perfluoroalkane sulfonyl fluorides non-covalently bind to human serum albumin at Sudlow's sites
- Authors:
- Jin, Zhe
Chi, Miao
He, Quan
Pan, Yuanjiang
Sun, Cuirong - Abstract:
- Highlights: Scarce toxicology study about PFASFs. Non-covalent interactions between HSA and PFASFs were proved. The association constants between HSA and PFASFs were determined. The binding numbers of PFASFs on HSA were measured by mass spectrometry. Abstract: Perfluorooctane sulfonyl fluoride (PFOSF) has been defined as persistent organic pollutant in the Stockholm Convention in 2009. Currently PFOSF and its substitutes (structural analogues in which octyl group is substituted for other aliphatic chains) are still scarcely studied. HSA is a main carrier for drugs in blood, and the influence of exogenous compounds including pollutants on HSA is of particular interest. In this work, the binding sites of HSA to Perfluoroalkane sulfonyl fluoride (PFASFs) were determined by fluorescence technique. The results demonstrated that PFASFs competitively bind to HSA at Sudlow's site I against warfarin and at Sudlow's site II against dansyl-proline and the related association constants were determined. The association constants of PFOSF, perfluorohexane sulfonyl fluoride (PFHSF) and perfluorobutane sulfonyl fluoride (PFBSF) were determined to be 2.59 × 10 −3 μM -1, 4.65 × 10 −3 μM -1 and 2.85 × 10 −3 μM -1 at Sudlow's site I and 8.68 × 10 −4 μM -1, 3.43 × 10 −2 μM -1 and 1.92 × 10 −2 μM -1 at Sudlow's site II, respectively. The results showed that PFASFs can bind tightly to HSA and thus migrate to all parts of the body through vascular system. Non-covalent interaction between HSAHighlights: Scarce toxicology study about PFASFs. Non-covalent interactions between HSA and PFASFs were proved. The association constants between HSA and PFASFs were determined. The binding numbers of PFASFs on HSA were measured by mass spectrometry. Abstract: Perfluorooctane sulfonyl fluoride (PFOSF) has been defined as persistent organic pollutant in the Stockholm Convention in 2009. Currently PFOSF and its substitutes (structural analogues in which octyl group is substituted for other aliphatic chains) are still scarcely studied. HSA is a main carrier for drugs in blood, and the influence of exogenous compounds including pollutants on HSA is of particular interest. In this work, the binding sites of HSA to Perfluoroalkane sulfonyl fluoride (PFASFs) were determined by fluorescence technique. The results demonstrated that PFASFs competitively bind to HSA at Sudlow's site I against warfarin and at Sudlow's site II against dansyl-proline and the related association constants were determined. The association constants of PFOSF, perfluorohexane sulfonyl fluoride (PFHSF) and perfluorobutane sulfonyl fluoride (PFBSF) were determined to be 2.59 × 10 −3 μM -1, 4.65 × 10 −3 μM -1 and 2.85 × 10 −3 μM -1 at Sudlow's site I and 8.68 × 10 −4 μM -1, 3.43 × 10 −2 μM -1 and 1.92 × 10 −2 μM -1 at Sudlow's site II, respectively. The results showed that PFASFs can bind tightly to HSA and thus migrate to all parts of the body through vascular system. Non-covalent interaction between HSA and PFASFs was confirmed with tryptic digestion experiment. The mass spectra results indicated that other binding sites of HSA are also involved in the binding of PFHSF and PFBSF. The total binding numbers of PFOSF, PFHSF and PFBSF on HSA are 2, 6 and 3, respectively. … (more)
- Is Part Of:
- Toxicology letters. Volume 301(2019)
- Journal:
- Toxicology letters
- Issue:
- Volume 301(2019)
- Issue Display:
- Volume 301, Issue 2019 (2019)
- Year:
- 2019
- Volume:
- 301
- Issue:
- 2019
- Issue Sort Value:
- 2019-0301-2019-0000
- Page Start:
- 17
- Page End:
- 23
- Publication Date:
- 2019-02
- Subjects:
- HSA -- Non-covalent interaction -- PFASFs -- Fluorescence -- MALDI
Toxicology -- Periodicals
363.179 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03784274 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.toxlet.2018.11.001 ↗
- Languages:
- English
- ISSNs:
- 0378-4274
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8873.042000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 9157.xml