Dissociation of arsenite-peptide complexes: Triphasic nature, rate constants, half-lives, and biological importance
✍ Scribed by Kirk T. Kitchin; Kathleen Wallace
- Publisher
- John Wiley and Sons
- Year
- 2006
- Tongue
- English
- Weight
- 205 KB
- Volume
- 20
- Category
- Article
- ISSN
- 1095-6670
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✦ Synopsis
Abstract
We determined the number and the dissociation rate constants of different complexes formed from arsenite and two peptides containing either one (RVCAVGNDYASGYHYGV for peptide 20) or three cysteines (LECAWQGK CVEGTEHLYSMKCK for peptide 10) via radioactive ^73^As‐labeled arsenite and vacuum filtration methodology. Nonlinear regression analysis of the dissociation of both arsenite‐peptide complexes showed that triphasic fits gave excellent r^2^ values (0.9859 for peptide 20 and 0.9890 for peptide 10). The first phase of arsenite‐peptide dissociation had the largest span (decrease in binding), and the rate was too fast to be measured using vacuum filtration methods. The dissociation rate constants of arsenite‐peptide complexes for the second phase were 0.35 and 0.54 min^−1^ and for the third phase were 0.0071 and 0.0045 min^−1^ for peptides 20 and 10, respectively. For peptide 20, the three spans of triphasic decay were 85%, 9%, and 7% of the total binding of 16.1 nmolsol;mg protein. For peptide 10, which can bind in both an intermolecular and intramolecular manner, the three spans of triphasic decay were 59%, 16%, and 25% of the total binding of 43.7 nmolsol;mg protein. Binding of trivalent arsenicals to peptides and proteins can alter their structure and function and contribute to adverse health outcomes such as toxicity and carcinogenicity. © 2006 Wiley Periodicals, Inc. *This article is a U.S. Government work and, as such, is in the public domain of the United States of America.
J Biochem Mol Toxicol 20:48–56, 2006; Published online in Wiley InterScience (www.interscience.wiley.com). DOI 10.1002/jbt.20108