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Conformational analysis of Na,K-ATPase in drug–protein complexes

Paper ID Volume ID Publish Year Pages File Format Full-Text
30376 44474 2008 8 PDF Available
Title
Conformational analysis of Na,K-ATPase in drug–protein complexes
Abstract

This review reports the effects of several drugs such as AZT (anti-AIDS), cis-Pt (antitumor), aspirin (anti-inflammatory) and vitamin C (antioxidant) on the stability and conformation of Na,K-ATPase in vitro. Drug–enzyme binding was found to be via H-bonding to the polypeptide CO and C–N groups with two binding constants K1(AZT) = 5.30 (±2.1) × 105 M−1 and K2(AZT) = 9.80 (±2.9) × 103 M−1 for AZT and one binding constant Kcis-Pt = 1.93 (±1.2) × 104 M−1 for cis-Pt, Kaspirin = 6.45 (±2.5) × 103 M−1 and Kascorbate = 1.04 (±0.5) × 104 M−1 for aspirin and ascorbic acid. The enzyme secondary structure was altered with major increase of α-helix from 19.9% (free protein) to 22–26% and reduction of β-sheet from 25.6% (free protein) to 17–23% upon drug complexation indicating a partial stabilization of protein conformation. The order of induced stability is AZT>cis-Pt > ascorbate > aspirin.

Keywords
ATPase; Drug; Binding constant; Secondary structure; UV–Visible; FTIR spectroscopy
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Photochemistry and Photobiology B: Biology - Volume 91, Issues 2–3, 29 May 2008, Pages 167–174
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
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Any Questions? feel free to contact us