Molecular interactions of benzophenone UV filters with human serum albumin revealed by spectroscopic techniques and molecular modeling

- We probed the interaction of four UV filters with human serum albumin (HSA).
- Four UV filters significantly quench intrinsic fluorescence of HSA via static mode.
- Significant structural changes of HSA occur upon the binding of UV filters.
- Two degradation products (BP-1 and BP-8) have higher binding affinities over BP-3.
- Our work helps to understand the risk assessment of BP-type UV filters.