US EPA

1487677 

Journal Article 

Investigations of acetaminophen binding to bovine serum albumin in the presence of fatty acid: Fluorescence and H-1 NMR studies 

Bojko, B; Sulkowska, A; Maciazek-Jurczyk, M; Rownicka, J; Sulkowski, WW 

2009 

1 

Journal of Molecular Structure: Theochem
ISSN: 0166-1280
EISSN: 1872-7999 

Elsevier 

AMSTERDAM 

924-26 

C 

332-337 

English 

10.1016/j.molstruc.2008.12.015 

WOS:000266574200053 

https://www.scopus.com/inward/record.uri?eid=2-s2.0-65049088244&doi=10.1016%2fj.molstruc.2008.12.015&partnerID=40&md5=579e738219bff4da1d5da20bbc8f8a2f
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The binding of acetaminophen to bovine serum albumin (BSA)
was studied by the quenching fluorescence method and the proton nuclear magnetic resonance
technique (H-1 NMR). For fluorescence measurements 1-anilino-9-naphthalene sulfonate (ANS)
hydrophobic probe was used to verify subdomain IIIA as acetaminophen's likely binding site.
Three binding sites of acetaminophen in subdomain IIA of bovine serum albumin were found.
Quenching constants calculated by the Stern-Volmer modified method were used to estimate the
influence of myristic acid (MYR) on the drug binding to the albumin. The influence of [fatty
acid]/[albumin] molar ratios on the affinity of the protein towards acetaminophen was described.
Changes of chemical shifts and relaxation times of the drug indicated that the presence of MYR
inhibits interaction in the AA-albumin complex. It is suggested that the elevated level of fatty
acids does not significantly influence the pharmacokinetics of acetaminophen. (C) 2008 Elsevier
B.V. All rights reserved. 

Acetaminophen; Fatty acid; ANS; NMR; Fluorescence 

JOURNAL OF MOLECULAR STRUCTURE