Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Bioorg Med Chem. 2010 Nov 1;18(21):7486-96. doi: 10.1016/j.bmc.2010.08.052. Epub 2010 Sep 24.

A combined spectroscopic and crystallographic approach to probing drug-human serum albumin interactions.

Author information

  • 1AstraZeneca, Alderley Park, Macclesfield, Cheshire SK104TG, England, United Kingdom.

Abstract

The displacement of probes that bind selectively to subdomains IIA or IIIA on human serum albumin (HSA) by competing compounds has been followed using fluorescence spectroscopy, and has therefore been used to assign a primary binding site for these compounds in the presence and absence of fatty acids. The crystal structures have also been solved for three compounds: a matched pair of carboxylic acids whose binding strength to HSA unexpectedly decreased as the lipophilicity increased; and a highly bound sulphonamide that appeared not to displace the probes in the displacement assay. The crystallography results support the findings from the fluorescence displacement assay. The results indicate that drug binding to subdomain IB might also be important location for certain compounds.

Copyright © 2010 Elsevier Ltd. All rights reserved.

PMID:
20869876
[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk