| Full text | |
| Author(s): |
Silva, Adriana Farias
[1]
;
Torossian Torres, Marcelo Der
[1]
;
Silva, Leandro de Souza
[2]
;
Alves, Flavio Lopes
[3]
;
de Sa Pinheiro, Ana Acacia
[2]
;
Miranda, Antonio
[3]
;
Capurro, Margareth Lara
[4]
;
Oliveira, Jr., Vani Xavier
[1]
Total Authors: 8
|
| Affiliation: | [1] Univ Fed ABC, Ctr Ciencias Nat & Humanas, BR-09210170 Santo Andre, SP - Brazil
[2] Univ Fed Rio de Janeiro, Inst Biofis Carlos Chagas Filho, BR-21941 Rio De Janeiro, RJ - Brazil
[3] Univ Fed Sao Paulo, Dept Biofis, Sao Paulo, SP - Brazil
[4] Univ Sao Paulo, Inst Ciencias Biomed 2, Dept Parasitol, Sao Paulo, SP - Brazil
Total Affiliations: 4
|
| Document type: | Journal article |
| Source: | Malaria Journal; v. 14, NOV 4 2015. |
| Web of Science Citations: | 3 |
| Abstract | |
Background: Antiplasmodial activities of angiotensin II and its analogues have been extensively investigated in Plasmodium gallinaceum and Plasmodium falciparum parasite species. Due to its vasoconstrictor property angiotensin II cannot be used as an anti-malarial drug. Methods: This work presents the solid-phase syntheses and liquid chromatography and mass spectrometry characterization of ten linear peptides related to angiotensin II against mature P. gallinaceum sporozoites and erythrocyte invasion by P. falciparum. Conformational analyses were performed by circular dichroism. IC50 assays were performed to identify the ideal concentration used on the biological tests and haemolytical erythrocytic assays were made to verify the viability of the biological experiments. The contractile responses of the analogues were made to evaluate if they are promising candidates to be applied as antiplasmodial drugs. Results: The results indicate two short-peptides constituted by hydrophobic residues (5 and 6) with antiplasmodial activity in these models, 89 and 94 % of biological activity against P. gallinaceum sporozoite, respectively, and around 50 % of activity against P. falciparum. Circular dichroism spectra suggested that all the peptides adopted beta-turn conformation in different solutions, except peptide 3. Besides the biological assays IC50, the haemolysis assays and contractile response activities were applied for peptides 5 and 6, which did not present expressive results. Conclusions: The hydrophobic portion and the arginine, tyrosine, proline, and phenylalanine, when present on peptide primary sequence, tend to increase the antiplasmodial activity. This class of peptides can be explored, as antimalarial drugs, after in vivo model tests. (AU) | |
| FAPESP's process: | 11/11348-2 - Antimalarial Peptides derivative from Angiotensin II |
| Grantee: | Adriana Farias da Silva |
| Support Opportunities: | Scholarships in Brazil - Doctorate |
| FAPESP's process: | 11/10823-9 - Antimalarial compounds derivative from angiotensin II |
| Grantee: | Vani Xavier de Oliveira Junior |
| Support Opportunities: | Regular Research Grants |
| FAPESP's process: | 14/12938-6 - Biologically active peptides against pathogenic micro-organisms |
| Grantee: | Vani Xavier de Oliveira Junior |
| Support Opportunities: | Regular Research Grants |