| Article ID | Journal | Published Year | Pages | File Type | 
|---|---|---|---|---|
| 1177620 | Analytical Biochemistry | 2006 | 7 Pages | 
Abstract
												Complexation of the hexapeptide Hys-Cys-Lys-Phe-Trp-Trp, inhibitor of the human immunodeficiency virus integrase protein, with the heavy metal ions Cd2+, Pb2+, and Zn2+ has been investigated using differential pulse polarography. In the case of Pb2+, no significant complexation is detected, whereas in the cases of Cd2+ and Zn2+, strong and electrochemically inert ML2 complexes predominate. In contrast, ML complexes are present in a low proportion or are absent. When possible, the corresponding conditional stability constants have been determined at both pH 7.0 and pH 7.5, showing that Zn2+ complexes are slightly more stable than Cd2+ complexes.
											Keywords
												
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													Physical Sciences and Engineering
													Chemistry
													Analytical Chemistry
												
											Authors
												Elena Chekmeneva, José Manuel DÃaz-Cruz, Cristina Ariño, Miquel Esteban, 
											