Amphiphilic Corroles Bind Tightly to Human Serum Albumin
Abstract
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.
Additional Information
© 2004 American Chemical Society. Received 30 September 2003; Published online 19 June 2004; Published in print 1 July 2004. Work at the Technion was supported by the STAR (Chicago) Foundation (Z.G.) and the Israel Science Foundation (Z.G.); work at Caltech was supported by JPL-NASA (K.S.) and the National Science Foundation (H.B.G., J.J.W.).Additional details
- Eprint ID
- 73706
- Resolver ID
- CaltechAUTHORS:20170125-093851899
- STAR Foundation
- Israel Science Foundation (ISF)
- NASA/JPL
- NSF
- Created
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2017-01-25Created from EPrint's datestamp field
- Updated
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2021-11-11Created from EPrint's last_modified field