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

Chamlian, Mayra; Bastos, E. L.; Maciel, Ceres; Capurro, Margareth Lara; Miranda, Antônio; Silva, Adriana F.; Torres, Marcelo Der Torossian; Oliveira, Vani Xavier

doi:10.1002/psc.2534

Cited by 21 publications

(37 citation statements)

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“…Conformational analysis of retro ‐AII indicated a randomly coiled conformation in all means evaluated. This might have led to reduced peptide–membrane interactions, in agreement with earlier studies that suggested that randomly coiled peptides show less effectiveness in the Plasmodium membrane disruption . The VC5 and all‐D ‐VC5 restricted analogs adopted predominantly a β‐turn conformation on all the means studied, and their antiplasmodial activity was consistently high.…”

Section: Resultssupporting

confidence: 88%

Evidences for the action mechanism of angiotensin II and its analogs onPlasmodiumsporozoite membranes

et al. 2016

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Malaria is an infectious disease responsible for approximately one million deaths annually. Oligopeptides such as angiotensin II (AII) and its analogs are known to have antimalarial effects against Plasmodium gallinaceum and Plasmodium falciparum. However, their mechanism of action is still not fully understood at the molecular level. In the work reported here, we investigated this issue by comparing the antimalarial activity of AII with that of (i) its diastereomer formed by only d-amino acids; (ii) its isomer with reversed sequence; and (iii) its analogs restricted by lactam bridges, the so-called VC5 peptides. Data from fluorescence spectroscopy indicated that the antiplasmodial activities of both all-D-AII and all-D-VC5 were as high as those of the related peptides AII and VC5, respectively. In contrast, retro-AII had no significant effect against P. gallinaceum. Conformational analysis by circular dichroism suggested that AII and its active analogs usually adopted a β-turn conformation in different solutions. In the presence of membrane-mimetic micelles, AII had also a β-turn conformation, while retro-AII was random. Molecular dynamics simulations demonstrated that the AII chains were slightly more bent than retro-AII at the surface of a model membrane. At the hydrophobic membrane interior, however, the retro-AII chain was severely coiled and rigid. AII was much more flexible and able to experience both straight and coiled conformations. We took it as an indication of the stronger ability of AII to interact with membrane headgroups and promote pore formation.

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Section: Resultssupporting

confidence: 88%

Evidences for the action mechanism of angiotensin II and its analogs onPlasmodiumsporozoite membranes

et al. 2016

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“…The substitution in a C-terminal extremity decreased peptide-parasite interaction (peptide 9 and peptide 10-70% and 73%, respectively). This behavior was observed by Chamlian, et al [7]. The antiplasmodial activity decreased in comparison to VIPF (analog 6), analog 7 and 8 had activity ≥ 75%.…”

Section: Resultssupporting

confidence: 69%

Linear Peptides Related to Angiotensin II with Antiplasmodial Activity

Silva¹,

Torres²,

Silva³

et al. 2015

Peptides 2015, Proceedings of the 24th American Peptide Symposium

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“…Based on the antiplasmodial activity reported by Maciel and Chamlian , we synthesized five AII‐restricted analogs that contained disulfide bridge cyclizations by inserting two Cys residues in the native sequence of the hormone.…”

Section: Resultsmentioning

confidence: 99%

Highly Potential Antiplasmodial Restricted Peptides

et al. 2014

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Malaria is an infectious disease responsible for approximately one million deaths annually. The antimalarial effects of angiotensin II and its analogs against Plasmodium gallinaceum and P. falciparum have recently been reported. To evaluate antiplasmodial activity, we synthesized five angiotensin II-restricted analogs containing disulfide bridges. To accomplish this, peptides containing two inserted amino acid residues (cysteine) were synthesized by the Fmoc solid-phase method, purified by liquid chromatography, and characterized by mass spectrometry. Conformational studies were performed by circular dichroism. The results indicated that two of the analogs had higher antiplasmodium activity (92% and 98% activity) than angiotensin II (88% activity), measured by fluorescence microscopy. Results showed that the insertion position must be selected, to preserve the hydrophobic interactions between the non-polar residues, as this affects antiplasmodial activity. The circular dichroism studies suggested that the active analogs as well as the native angiotensin II adopt a β-turn conformation in different solutions. This approach provided insight for understanding the effects of restricting the ring size and position on the bioactivity of angiotensin II and provides a new direction for the design of potential chemotherapeutic agents.

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

Cited by 21 publications

References 50 publications

Evidences for the action mechanism of angiotensin II and its analogs onPlasmodiumsporozoite membranes

Evidences for the action mechanism of angiotensin II and its analogs onPlasmodiumsporozoite membranes

Linear Peptides Related to Angiotensin II with Antiplasmodial Activity

Highly Potential Antiplasmodial Restricted Peptides

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