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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

A study of the anti-plasmodium activity of angiotensin II analogs

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Author(s):
Chamlian, Mayra [1] ; Bastos, Erick L. [2] ; Maciel, Ceres [3] ; Capurro, Margareth L. [3] ; Miranda, Antonio [4] ; Silva, Adriana F. [1] ; Torres, Marcelo Der T. [1] ; Oliveira, Jr., Vani X. [1]
Total Authors: 8
Affiliation:
[1] Univ Fed ABC, Ctr Ciencias Nat & Humanas, BR-09210170 Santo Andre, SP - Brazil
[2] Univ Sao Paulo, Inst Quim, Dept Quim Fundamental, Sao Paulo - Brazil
[3] Univ Sao Paulo, Inst Ciencias Biomed, BR-05508 Sao Paulo - Brazil
[4] Univ Fed Sao Paulo, Dept Biofis, Sao Paulo - Brazil
Total Affiliations: 4
Document type: Journal article
Source: JOURNAL OF PEPTIDE SCIENCE; v. 19, n. 9, p. 575-580, SEP 2013.
Web of Science Citations: 17
Abstract

Controlling the dissemination of malaria requires the development of new drugs against its etiological agent, a protozoan of the Plasmodium genus. Angiotensin II and its analog peptides exhibit activity against the development of immature and mature sporozoites of Plasmodium gallinaceum. In this study, we report the synthesis and characterization of angiotensin II linear and cyclic analogs with anti-plasmodium activity. The peptides were synthesized by a conventional solid-phase method on Merrifield's resin using the t-Boc strategy, purified by RP-HPLC and characterized by liquid chromatography/ESI (+) MS (LC-ESI(+)/MS), amino acid analysis, and capillary electrophoresis. Anti-plasmodium activity was measured in vitro by fluorescence microscopy using propidium iodine uptake as an indicator of cellular damage. The activities of the linear and cyclic peptides are not significantly different (p<0.05). Kinetics studies indicate that the effects of these peptides on plasmodium viability overtime exhibit a sigmoidal profile and that the system stabilizes after a period of 1h for all peptides examined. The results were rationalized by partial least-square analysis, assessing the position-wise contribution of each amino acid. The highest contribution of polar amino acids and a Lys residue proximal to the C-terminus, as well as that of hydrophobic amino acids in the N-terminus, suggests that the mechanism underlying the anti-malarial activity of these peptides is attributed to its amphiphilic character. Copyright (c) 2013 European Peptide Society and John Wiley \& Sons, Ltd. (AU)

FAPESP's process: 07/00684-6 - Synthesis and application of modified flower pigments
Grantee:Erick Leite Bastos
Support type: Research Grants - Young Investigators Grants