Comparison of nonmetal and metal hydrophilic photosensitizer, ATX-S10 (Na) and ATN-2, binding with human serum proteins using spectrophotometry.
Intermolecular interactions of human serum proteins with a hydrophilic nonmetalloporphyrin, 13,17-bis(1-carboxypropionyl)carbomoylethyl-8-ethenyl-2-hydroxy-3-hydroxyiminoethylidene-2,7,12,18-tetramethylporphyrin sodium salt (ATX-S10 (Na)), or a hydrophilic gallium-metalloporphyrin, diethylenetriamine pentaacetic acid ester of 2-[1-(2-hydroxy-ethoxy)ethyl]-4-vinyl-deuteroporphyrin (IX) Ga complex (ATN-2), were investigated using spectrophotometry. ATX-S10 (Na) caused a bathochromic shift with albumin, high-density lipoprotein and low-density lipoprotein, but little or no shift was observed with hemopexin, transferrin and immunoglobulin G. In contrast, ATN-2 displayed a bathochromic shift only with hemopexin. These results suggest that the association energy of ATX-S10 (Na) with albumin might be slightly greater than that with lipoproteins and that of ATN-2 with hemopexin might be greater than that with other serum proteins.
Department of Veterinary Clinical Science, Obihiro University of Agriculture and Veterinary Medicine, Obihiro-City, Hokkaido, Japan.
M
M
Yamaguchi
S
S
Tanabe
S
S
Nakajima
T
T
Takemura
K
K
Ogita
H
H
Kuwayama
I
I
Sakata
S
S
Miyaki
K
K
Suzuki
H
H
Namiki
Y
Y
Uzuka
T
T
Sarashina
D001798:Blood Proteins / Q000737:chemistry*; D005708:Gallium / Q000737:chemistry*; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D015394:Molecular Structure; D017319:Photosensitizing Agents / Q000737:chemistry*; D011166:Porphyrins / Q000737:chemistry*; D013053:Spectrophotometry
C115550:ATX-S10; D001798:Blood Proteins; D017319:Photosensitizing Agents; D011166:Porphyrins; C057315:ATN-2; D005708:Gallium