Differential scanning fluorimetry to assess PFAS binding to bovine serum albumin protein

被引:5
作者
Alesio, Jessica [1 ]
Bothun, Geoffrey D. [1 ]
机构
[1] Univ Rhode Isl, Dept Chem Engn, Kingston, RI 02881 USA
关键词
PERFLUOROALKYL ACIDS; THERMAL SHIFT; DAIRY-COWS; FLUORESCENCE; PFOA; ABSORPTION; MODEL;
D O I
10.1038/s41598-024-57140-9
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The rapid screening of protein binding affinity for poly- and perfluoroalkyl substances (PFAS) benefits risk assessment and fate and transport modelling. PFAS are known to bioaccumulate in livestock through contaminated food and water. One excretion pathway is through milk, which may be facilitated by binding to milk proteins such as bovine serum albumin (BSA). We report a label-free differential scanning fluorimetry approach to determine PFAS-BSA binding over a broad temperature range. This method utilizes the tryptophan residue within the protein binding pocket as an intrinsic fluorophore, eliminating the need for fluorophore labels that may influence binding. BSA association constants were determined by (a) an equilibrium-based model at the melting temperature of BSA and (b) the Hill adsorption model to account for temperature dependent binding and binding cooperativity. Differences in binding between PFAS and fatty acid analogs revealed that a combination of size and hydrophobicity drives PFAS binding.
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页数:9
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