Amphiphilic corroles bind tightly to human serum albumin.
Amphiphilic 2,17-bis-sulfonato-5,10,15(trispentafluorophenyl)corrole (2) and its Ga and Mn complexes (2-Ga and 2-Mn) form tightly bound noncovalent conjugates with human serum albumin (HSA). Protein-induced changes in the electronic absorption, emission, and circular dichroism spectra of these corroles, as well as results obtained from HPLC profiles of the conjugates and selective fluorescence quenching of the single HSA tryptophan, are interpreted in terms of multiple corrole:HSA binding sites. High-affinity binding sites, close to the unique tryptophan, are fully occupied at very low concentrations. At biologically relevant HSA concentrations (2-3 orders of magnitude larger than those employed in our studies), all corroles (2, 2-Ga, and 2-Mn) may be considered as fully conjugated.
Mahammed
Atif
A
Department of Chemistry, Technion - Israel Institute of Technology, Haifa 32,000.
Gray
Harry B
HB
Weaver
Jeremy J
JJ
Sorasaenee
Karn
K
Gross
Zeev
Z
D001665:Binding Sites; D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D005453:Fluorescence; D006801:Humans; D008958:Models, Molecular; D015394:Molecular Structure; D011166:Porphyrins / Q000737:chemistry*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012709:Serum Albumin / Q000737:chemistry*; D013057:Spectrum Analysis; D017186:Titrimetry
D011166:Porphyrins; D012709:Serum Albumin; C431863:corrole