Curcuminoids are a class of photoactive organic compounds that have practical applications as photosensitizers in photodynamic drug therapy (PDT). PDT is an alternative cancer therapy that targets a specific treatment region using a photosensitizer to create reactive oxygen species, which cause cellular apoptosis of cancer cells. This research focuses on the binding relationship between human serum albumin (HSA), a common drug carrying protein in the human blood, and various curcumin derivatives. The derivatives used in this study were differentiated by the substituent groups (-OCH<sub>3</sub>, -OH, -H) on the aromatic rings, which resulted in varied molecular polarity. Observations from homogeneous, binding, and quenching studies show that all curcuminiods bind to HSA. However, the more polar curcuminoids such as didemethyl curcumin and bisdemethoxycurcumin are observed to have a greater binding affinity toward the tryptophan site found in subdomain IIA in HSA, while the non-polar curcuminoiods have a lower binding affinity for HSA. These results indicate that the curcumin derivatives show great potential for use as photosensitizers in PDT.

Analysis of the binding relationship between curcumin derivatives and human serum albumin by steady-state fluorescence spectroscopy

2019 Spring National Meeting

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