Molecular interaction and energy transfer between human serum albumin and polyoxometalates

The technique of circular dichroism (CD) is employed to study the molecular interaction and mechanistic pathways governing the interaction between the fatty-acid-free human serum albumin (HSA) and various polyoxometalates (POMs). The analysis reveals that different POMs have different effects on the secondary nature of the protein, though the excited-state lifetime of the single tryptophan molecule is drastically reduced after the binding.