Crystallographic analysis reveals the structural basis of the high-affinity binding of iophenoxic acid to human serum albumin.

ABSTRACT:

Background

Iophenoxic acid is an iodinated radiocontrast agent that was withdrawn from clinical use because of its exceptionally long half-life in the body, which was due in part to its high-affinity binding to human serum albumin (HSA). It was replaced by Iopanoic acid, which has an amino rather than a hydroxyl group at position 3 on the iodinated benzyl ring and, as a result, binds to albumin with lower affinity and is excreted more rapidly from the body. To understand how iophenoxic acid binds so tightly to albumin, we wanted to examine the structural basis of its interaction with HSA.

Results

We have determined the co-crystal structure of HSA in complex with iophenoxic acid at 2.75 Å resolution, revealing a total of four binding sites, two of which--in drugs sites 1 and

SUBMITTER: Ryan AJ 

PROVIDER: S-EPMC3104944 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature