Comparison of nonmetal and metal hydrophilic photosensitizer, ATX-S10 (Na) and ATN-2, binding with human serum proteins using spectrophotometry.

Abstract:

: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.

journal_name

Photochem Photobiol

authors

Yamaguchi M,Tanabe S,Nakajima S,Takemura T,Ogita K,Kuwayama H,Sakata I,Miyaki S,Suzuki K,Namiki H,Uzuka Y,Sarashina T

doi

10.1562/2004-03-17-RA-117

subject

Has Abstract

pub_date

2004-09-01 00:00:00

pages

262-6

issue

2

eissn

0031-8655

issn

1751-1097

pii

2004-03-17-RA-117

journal_volume

80

pub_type

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