Photophysical Studies on the Supramolecular Photochirogenesis for the Photocyclodimerization of 2-Anthracenecarboxylate within Human Serum Albumin

• Published in: The journal of physical chemistry. B Vol. 113; no. 30; pp. 10445 - 10453
• Main Authors: Pace, Tamara C. S, Nishijima, Masaki, Wada, Takehiko, Inoue, Yoshihisa, Bohne, Cornelia
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 30.07.2009
• Subjects: Anthracenes - chemistry; Anthracenes - metabolism; B: Biophysical Chemistry; Binding Sites; Binding, Competitive; Carboxylic Acids - chemistry; Carboxylic Acids - metabolism; Humans; Iodobenzoates - metabolism; Iodobenzoates - pharmacology; Methane - analogs & derivatives; Methane - metabolism; Methane - pharmacology; Nitroparaffins - metabolism; Nitroparaffins - pharmacology; Photolysis; Serum Albumin - antagonists & inhibitors; Serum Albumin - metabolism; Spectrometry, Fluorescence; Stereoisomerism; Substrate Specificity; Time Factors
• ISSN: 1520-6106; 1520-5207
• DOI: 10.1021/jp903955f

The mechanism for the chirogenesis in the photocyclodimerization of 2-anthracenecarboxylate (AC) bound to human serum albumin (HSA) was investigated using time-resolved fluorescence measurements in the presence of HSA inhibitors and/or an AC singlet excited state quencher. The photophysical studies were correlated with product studies to explain the high enantiomeric excess (ee) observed for the chiral photoproducts. AC binds to HSA in five different binding sites with decreasing affinities. AC bound to the sites with the highest affinity (sites 1 and 2) is unreactive, and the AC can be displaced from these sites by the use of known inhibitors. Time-resolved fluorescence studies isolated a singlet excited state AC bound to a site which exhibited moderate protection from interactions with species in the aqueous phase. This site was assigned to binding site 3, where the chiral photoproducts are formed with a high ee based on the correlation of the photophysical studies with product studies in the presence of a quencher. These results show that the use of inhibitors for multiple binding site proteins is useful to uncover the properties of binding sites for which guest binding has only moderate affinity and where the photophysical characterization of these binding sites is not possible in the absence of inhibitors.