Arsenic trioxide binding to serum proteins

Arsenic trioxide binding to serum proteins

Arsenic trioxide (ATO) also known as Trisenox, is an anticancer chemotherapeutic drug which has been used in treating diagnosed and relapsed patients with acute promyelocytic leukemia (APL). Serum albumin is the most abundant of the proteins in blood plasma and is the major transporter for deliverin...

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Bibliographic Details
Published in:Journal of photochemistry and photobiology. B, Biology Vol. 148; pp. 31 - 36
Main Authors: Shooshtary, Sara, Behtash, Sima, Nafisi, Shohreh
Format: Journal Article
Language:English
Published: Switzerland 01-07-2015
Subjects:
Animals
Arsenicals - chemistry
Arsenicals - metabolism
Cattle
Humans
Oxides - chemistry
Oxides - metabolism
Protein Binding
Protein Structure, Secondary
Protein Structure, Tertiary
Serum Albumin - chemistry
Serum Albumin - metabolism
Serum Albumin, Bovine - chemistry
Serum Albumin, Bovine - metabolism
Spectrophotometry, Ultraviolet
Spectroscopy, Fourier Transform Infrared
Bovine serum albumin
Human serum albumin
Arsenic trioxide
FT-IR
UV–Vis spectroscopy
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Summary:Arsenic trioxide (ATO) also known as Trisenox, is an anticancer chemotherapeutic drug which has been used in treating diagnosed and relapsed patients with acute promyelocytic leukemia (APL). Serum albumin is the most abundant of the proteins in blood plasma and is the major transporter for delivering several drugs in vivo. The current study was designed to evaluate the potential ability of human and bovine serum albumin for delivering arsenic trioxide. Therefore, interaction of arsenic trioxide with HSA and BSA was investigated in aqueous solution at physiological conditions using a constant protein concentration and various drug contents. FTIR and UV-Vis spectroscopic methods were used to analyze arsenic trioxide and protein binding modes, the binding constants and the effect of drug complexation on HSA and BSA stability and conformation. Results of this study showed that drug complexation altered protein conformation by major reduction of α-helix and increase of turn structure which is indicative of a partial protein destabilization. Structural analysis revealed that arsenic trioxide bind HSA and BSA with overall binding constants of KATO-HSA=1.07 (±0.01)×10(4) M(-1) and KATO-BSA=1.27(±0.02)×10(4) M(-1). It could be concluded that serum albumins can be considered as good carriers for delivering arsenic trioxide to target tissue.
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ISSN:1011-1344
1873-2682
DOI:10.1016/j.jphotobiol.2015.03.001