logo

Metal-Based Drugs

PDF
Metal-Based Drugs / 1995 / Article

Open Access

Volume 2 |Article ID 297356 | https://doi.org/10.1155/MBD.1995.233

Juan Zou, Fang An, Gang Liu, Kui Wang, "The Binding of Platinum (II) Complexes to Rabbit Skeletal Muscle G-Actin Induces Conformation Changes", Metal-Based Drugs, vol. 2, Article ID 297356, 8 pages, 1995. https://doi.org/10.1155/MBD.1995.233

The Binding of Platinum (II) Complexes to Rabbit Skeletal Muscle G-Actin Induces Conformation Changes

Juan Zou,1 Fang An,2 Gang Liu,3 and Kui Wang3

1State Key Laboratory of Coordination Chemistry, Nanjing University, China

2Inorganic Chemistry Department, Zhang Jiakou Medical University, China

3Inorganic Chemistry Department, Beijing Medical University, School of Pharmaceutical Sciences, China

Received12 Jun 1995
Accepted05 Jul 1995

Abstract

The binding of cis-diamminedichloroplatinum (DDCP) and cis-diaquodiammine platinum (DADP) to rabbit skeletal muscle G-actin and the consequent conformation changes were studied as the function of the Pt/actin molar ratio (R) and time by intrinsic and NPM labeled fluorescence, CD spectra as well as gelfiltration chromatography. The results indicated that the unhydrolyzed DDCP can react with G-actin in presence of Cl- ion. The reaction differs from that of its hydrolysis product DADP in a higher specificity and a lower capacity. Both of them induced exposure of the tryptophane residues and labeled Cys374 and the increase in α-helix content depending on R, but the conformation changes caused by DADP are more significant than DDCP at the same R. These are related to the binding of DADP to groups other than thiols. The rate constants of conformation change suggested that DADP quenched the intrinsic fluorescence more rapid. The temporal change in fluorescence of NPM labeled actin has a biphasic feature: in the first 16 minutes, the fluorescence was quenched, then it recovered slowly, indicating a multi-step reaction including high affinity platinum binding → labeled Cys374 moving to hydrophilic environment → low affinity platinum binding → Cys374-related conformation compacting in sequence.

Copyright © 1995 Hindawi Publishing Corporation. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

More related articles

No related content is available yet for this article.
PDF Download Citation Citation
Order printed copiesOrder
Views66
Downloads42
Citations

Article of the Year Award: Outstanding research contributions of 2020, as selected by our Chief Editors. Read the winning articles.