| Full text | |
| Author(s): |
de Almeida, Fernando G.
;
Vanzolini, Kenia L.
;
Cass, Quezia B.
Total Authors: 3
|
| Document type: | Journal article |
| Source: | Journal of Pharmaceutical and Biomedical Analysis; v. 132, p. 159-164, JAN 5 2017. |
| Web of Science Citations: | 8 |
| Abstract | |
Angiotensin converting enzyme (ACE) presents an important role in blood pressure regulation, since that converts angiotensin I to the vasoconstrictor angiotensin II. Some commercially available ACE inhibitors are captopril, lisinopril and enalapril; due to their side effects, naturally occurring inhibitors have been prospected. In order to endorse this research field we have developed a new tool for ACE ligand screening. To this end, ACE was extracted from bovine lung, purified and chemically immobilized in modified ferrite magnetic beads (ACE-MBs). The ACE-MBs have shown a Michaelian kinetic behavior towards hippuryl-histidyl-leucine. Moreover, as proof of concept, the ACE-MBs was inhibited by lisinopril with a half maximal inhibitory concentration (IC50) of 10 nM. At the fishing assay, ACE-MBs were able not only to fish out the reference inhibitor, but also one peptide from a pool of tryptic digested BSA. In conclusion, ACE-MBs emerge as new straightforward tool for ACE kinetics determination, inhibition and binder screening. (C) 2016 Elsevier B.V. All rights reserved. (AU) | |
| FAPESP's process: | 13/01710-1 - Enzyme ligand: new models of screening |
| Grantee: | Quezia Bezerra Cass |
| Support Opportunities: | Research Projects - Thematic Grants |
| FAPESP's process: | 11/00398-9 - Angiotensin Converting Enzyme: from its immobilization to the natural inhibitors screening |
| Grantee: | Fernando Gonçalves de Almeida |
| Support Opportunities: | Scholarships in Brazil - Doctorate |