207
Views
14
CrossRef citations to date
0
Altmetric
Original Articles

Study on the Interaction between the Inclusion Complex of Hematoxylin with β-Cyclodextrin and DNA

, , &
Pages 854-866 | Received 13 Aug 2010, Accepted 11 Oct 2010, Published online: 01 Dec 2010
 

Abstract

Ultraviolet-visible (UV-vis) spectra, fluorescence spectra, electrochemistry, and the thermodynamic method were used to discuss the interaction mode between the inclusion complex of hematoxylin with β-cyclodextrin and herring sperm DNA. On the condition of physiological pH, the result showed that hematoxylin and β-cyclodextrin formed an inclusion complex with binding ratio nhematoxylin:nβ-cyclodextrin = 1:1. The interaction mode between β-cyclodextrin-hematoxylin and DNA was a mixed binding, which contained intercalation and electrostatic mode. The binding ratio between β-cyclodextrin-hematoxylin and DNA was nβ-cyclodextrin -hematoxylin:nDNA = 2:1, binding constant was K 298.15K = 5.29 × 104 L·mol−1, and entropy worked as driven force in this action.

Acknowledgments

This work was supported by the National Natural Science Foundation of China (No. 30973634) and Postgraduate Innovation Foundation of Southwest University of Science and Technology. The authors are grateful for the apparatus support of the Analytical and Testing Center of Southwest University of Science and Technology.

Log in via your institution

Log in to Taylor & Francis Online

PDF download + Online access

  • 48 hours access to article PDF & online version
  • Article PDF can be downloaded
  • Article PDF can be printed
USD 61.00 Add to cart

Issue Purchase

  • 30 days online access to complete issue
  • Article PDFs can be downloaded
  • Article PDFs can be printed
USD 606.00 Add to cart

* Local tax will be added as applicable

Related Research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.