1 research outputs found
Explaining the Highly Enantiomeric Photocyclodimerization of 2‑Anthracenecarboxylate Bound to Human Serum Albumin Using Time-Resolved Anisotropy Studies
The mechanism for the high enantiomeric excess (ee) (80–90%)
observed in the photocyclodimerization of 2-anthracenecarboxylate
(AC) in the chiral binding sites of human serum albumin (HSA) was
studied using fluorescence anisotropy. A long rotational correlation
time of 36 ns was observed for the excited states of the ACs bound
to the HSA site responsible for the high ee, suggesting that the ACs
have restricted rotational mobility in this site. The ACs in this
site have the same prochiral face protected by the protein, and this
protection is responsible for the high ee observed. These insights
provide a strategy for the rational design of supramolecular photochirogenic
systems