Enantioselective regulation of a metal complex in reversible binding to serum albumin: dynamic helicity inversion signalled by circularly polarised luminescence.
The helicity of the (SSS)-Delta enantiomer of a terbium and europium(III) complex is inverted on reversible binding to 'drug site II' of serum albumin, signalled by a switch in its circularly polarised emission; no such behaviour occurs with the (RRR)-Lambda complexes, thereby defining a unique chiroptical probe of albumin binding.
Montgomery
Craig P
CP
Department of Chemistry, Durham University, South Road, Durham, UK DH1 3LE.
New
Elizabeth J
EJ
Parker
David
D
Peacock
Robert D
RD
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D005063:Europium / Q000737:chemistry*; D049449:Luminescence; D008163:Luminescent Measurements; D008968:Molecular Conformation; D009942:Organometallic Compounds / Q000737:chemistry*; D012710:Serum Albumin, Bovine / Q000737:chemistry*; D013237:Stereoisomerism; D013329:Structure-Activity Relationship; D013725:Terbium / Q000737:chemistry*
D009942:Organometallic Compounds; D013725:Terbium; D012710:Serum Albumin, Bovine; D005063:Europium