Enantioselective quenching of the room-temperature phosphorescence RTP lifetime of proteins was demonstrated due to the effects of various external chiral quenching agents. In the absence of quenchers, the RTP lifetimes for bovine serum albumin BSA and human serum albumin HSA were found to be 5.0 ± 0.2 and 4.0 ± 0.1 ms, respectively. The addition of various chiral quenchers three pairs of binaphthols and two pairs of β-blockers into the deoxygenated sample solutions containing BSA and HSA reduced their RTP lifetimes significantly, i.e., from ca. 4-5 ms in the absence to an average lifetime of ca. 1-2 ms in the presence of the chiral quenchers. For the R and S enantiomers examined, marked differences in RTP lifetimes were observed, i.e., ranging from ca. 20-29% for the binaphthols to ca. 14-16% for the β-blockers. Such findings could lead to a better understanding of the relationship between chirality, dynamics/conformational changes, and biological functions of proteins.
|Number of pages||4|
|Publication status||Published - Mar 2007|
Scopus Subject Areas
- Polymers and Plastics
- Materials Chemistry