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In vitro binding of leukotriene B4 (LTB4) to human serum albumin: Evidence from spectroscopic, molecular modeling, and competitive displacement studies by Ferenc Zsila; Zsolt Bikádi; Samuel F. Lockwood is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Circular dichroism (CD) and UV absorption spectroscopy were utilized for the first time to investigate the interaction between leukotriene B 4 (LTB 4 ) and human serum albumin (HSA) in vitro. The weak intrinsic CD signal of LTB 4 was enhanced fivefold in the presence of HSA. The red-shifted, hypochromic, and reduced vibrational fine structure of the ligand/protein UV absorption spectrum indicated complexation of the two molecules in solution. Results obtained from CD titration experiments were subjected to non-linear regression analysis to estimate the binding parameters (K a = 6.7 • 10 4 M À1 , n = 1). Palmitic acid strongly decreased the induced CD signal of the LTB 4 /HSA complex, suggesting the role of a high-affinity fatty acid HSA binding site in the leukotriene complexation. Molecular modeling calculations based on the crystal structure of HSA predicted that the long-chain fatty acid site that overlaps with drug binding site II in subdomain IIIA was the most likely binding location for LTB 4 . Using the drug site II-specific marker ligand rac-ibuprofen, this prediction was confirmed with induced-CD displacement measurements. To the authorsÕ knowledge, the current study repre

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Author

Ferenc Zsila; Zsolt Bikádi; Samuel F. Lockwood

Publisher

Elsevier Science; Elsevier ; Elsevier Ltd.; Elsevier BV (ISSN 0960-894X)

Published

2005

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)