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Published on: October 16, 2015
Phenanthrene binding by humic acid-protein complexes as studied by passive dosing technique
Jian Zhao1, Zhenyu Wang, Saikat Ghosh
1Stockbridge School of Agriculture, University of Massachusetts, Amherst, MA 01003, USA.
Phenanthrene binding to humic substances and proteins was studied. Humic acid-bovine serum albumin complexes significantly enhanced phenanthrene binding, unlike other protein complexes.
Area of Science:
- Environmental Chemistry
- Biogeochemistry
- Organic Geochemistry
Background:
- Polycyclic aromatic hydrocarbons (PAHs) like phenanthrene are persistent organic pollutants.
- Humic substances (HS) and proteins are key environmental components influencing PAH fate.
- Understanding binding interactions is crucial for predicting PAH bioavailability and transport.
Purpose of the Study:
- To investigate phenanthrene binding to humic acids (HA) and proteins (bovine serum albumin (BSA), lysozyme, pepsin).
- To evaluate the binding behavior of phenanthrene with HA-protein complexes.
- To elucidate the mechanisms behind altered binding in complex matrices.
Main Methods:
- Passive dosing technique was employed to measure phenanthrene sorption.
- Sorption isotherms were analyzed using the Freundlich model.
- Binding affinities were compared across individual components and their complexes.
Main Results:
- Binding affinity order: HA-5 > HA-2 > BSA > pepsin > lysozyme.
- Phenanthrene binding to HA-BSA complexes was significantly enhanced compared to individual components.
- HA-lysozyme complexes showed reduced binding due to aggregation; HA-pepsin showed no enhancement.
Conclusions:
- Humic acid-protein complexation, particularly with BSA, can significantly increase phenanthrene binding.
- Protein unfolding, reduced aggregate size, and favorable complex conformations drive binding enhancement.
- The nature of the protein (charge, aggregation tendency) critically influences binding interactions.
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