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Interaction of human protein disulfide isomerase and human P5 with drug compounds: Analysis using biosensor technology

Paper ID Volume ID Publish Year Pages File Format Full-Text
35746 45105 2008 8 PDF Available
Title
Interaction of human protein disulfide isomerase and human P5 with drug compounds: Analysis using biosensor technology
Abstract

Binding of aminoglycoside antibiotics to protein disulfide isomerase (PDI) is known to inhibit the chaperone activity but not the isomerase activity of PDI. The amino sugar moiety of the antibiotics is a key factor in these interactions. In the present study, domain deletion analysis of human PDI (hPDI) revealed that the a′c domain is significant for binding to aminoglycoside antibiotics; however, other domains, including the a, b, and b′ domains, are also required, as assessed using the Biacore biosensor analysis system. It was found that the drug compounds interacting with the hPDI family of proteins can be classified into four groups according to the recognition motif for hPDI and hP5. The anti-cancer drug vincristine was found to inhibit chaperone activity but not isomerase activity for both hPDI and hP5 in vitro. Interestingly, a 100:1 molar ratio of vincristine to hPDI or hP5 was sufficient to almost completely inhibit the chaperone activity of hPDI and hP5. These findings may be useful not only for future structure–function studies of the PDI family of proteins but also for new drug design, since PDI plays a critical role in protein-folding in the endoplasmic reticulum and is indispensable for cell viability.

Keywords
hPDI, human protein disulfide isomerase; hP5, human P5; SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electrophoresis; DMSO, dimethyl sulfoxide; NADPH, nicotinamide adenine dinucleotide phosphate, reduced form; T3, 3,3′,5-triiodo-l-thyronine; MTX, m
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Interaction of human protein disulfide isomerase and human P5 with drug compounds: Analysis using biosensor technology
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 43, Issue 12, December 2008, Pages 1330–1337
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us