Corroles that bind with high affinity to both apo and holo transferrin.
The interactions of transferrin (Tf) with the water soluble corrole 1 and with its gallium (1-Ga) and manganese (1-Mn) complexes were studied to establish the possible utilization of corrole-transferrin conjugates for targeting these corroles to cells that express the transferrin receptor. The protein, in both its iron-free apo form (apoTf) and the iron-bound holo form (holoTf), was found to spontaneously bind all three derivatives. This conclusion was reached from titrations followed by several spectroscopic methods and dilution experiments measured by fluorescence. The such elucidated very small dissociation constant of 2 x 10(-7) M and 3 x 10(-8) M for 1-Ga with apoTf and holoTf, respectively and <10(-9) M for 1 with both protein forms are clearly relevant for the physiological concentration of transferrin in serum.
Haber
Adi
A
Schulich Faculty of Chemistry, Technion - Israel Institute of Technology, Haifa 32000, Israel.
Agadjanian
Hasmik
H
Medina-Kauwe
Lali K
LK
Gross
Zeev
Z
D004591:Electrophoresis, Polyacrylamide Gel; D005708:Gallium / Q000737:chemistry / Q000378:metabolism; D008274:Magnesium / Q000737:chemistry / Q000378:metabolism; D015394:Molecular Structure; D011166:Porphyrins / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D012044:Regression Analysis; D014168:Transferrin / Q000737:chemistry* / Q000378:metabolism*
D011166:Porphyrins; D014168:Transferrin; C431863:corrole; D005708:Gallium; D008274:Magnesium