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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.)

Antiplasmodial activity study of angiotensin II via Ala scan analogs

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Author(s):
Silva, Adriana Farias [1] ; Bastos, Erick Leite [2] ; Torres, Marcelo Der Torossian [1] ; Costa-da-Silva, Andre Luis [3] ; Ioshino, Rafaella Sayuri [3] ; Capurro, Margareth Lara [3] ; Alves, Flavio Lopes [4] ; Miranda, Antonio [4] ; Fischer Vieira, Renata de Freitas [4] ; Oliveira, Jr., Vani Xavier [1]
Total Authors: 10
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, Dept Parasitol, 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. 20, n. 8, p. 640-648, AUG 2014.
Web of Science Citations: 12
Abstract

Angiotensin II (AII) as well as analog peptides shows antimalarial activity against Plasmodium gallinaceum and Plasmodium falciparum, but the exact mechanism of action is still unknown. This work presents the solid-phase synthesis and characterization of eight peptides corresponding to the alanine scanning series of AII plus the amide-capped derivative and the evaluation of the antiplasmodial activity of these peptides against mature P. gallinaceum sporozoites. The Ala screening data indicates that the replacement of either the Ile(5) or the His(6) residues causes minor effects on the in vitro antiplasmodial activity compared with AII, i.e. AII (88%), {[}Ala(6)]-AII (79%), and {[}Ala(5)]-AII (75%). Analogs {[}Ala(3)]-AII, {[}Ala(1)]-AII, and AII-NH2 showed antiplasmodial activity around 65%, whereas the activity of the {[}Ala(8)]-AII, {[}Ala(7)]-AII, {[}Ala(4)]-AII, and {[}Ala(2)]-AII analogs is lower than 45%. Circular dichroism data suggest that AII and the most active analogs adopt a beta-fold conformation in different solutions. All AII analogs, except {[}Ala(4)]-AII and {[}Ala(8)]-AII, show contractile responses and interact with the AT(1) receptor, {[}Ala(5)]-AII and {[}Ala(6)]-AII. In conclusion, this approach is helpful to understand the contribution of each amino acid residue to the bioactivity of AII, opening new perspectives toward the design of new sporozoiticidal compounds. Copyright (C) 2014 European Peptide Society and John Wiley \& Sons, Ltd. (AU)

FAPESP's process: 11/23036-5 - Floral betalamic pigments: fluorescence and antiradical capacity
Grantee:Erick Leite Bastos
Support type: Regular Research Grants
FAPESP's process: 11/10823-9 - Antimalarial compounds derivative from angiotensin II
Grantee:Vani Xavier de Oliveira Junior
Support type: Regular Research Grants