Skip to main content

Advertisement

Log in

Recombinant C-Terminal Domains from Scorpine-like Peptides Inhibit the Plasmodium berghei Ookinete Development In Vitro

  • Published:
International Journal of Peptide Research and Therapeutics Aims and scope Submit manuscript

Abstract

Malaria is a parasitic disease, caused by protozoa of the genus Plasmodium, and is transmitted to humans through the bites of infected Anopheles mosquitoes. More than 200 million cases of malaria are reported annually and about 400,000 deaths worldwide. Currently, the use of antimalarial drugs has been efficient in most cases, however, resistance to these drugs is increasing, making it necessary and essential to have a new range of possible drugs or medicines to combat this disease. Scorpion venom contains peptides whose functions are now intensively studied. Some of these peptides are known as Scorpine-like, which have anti-bacterial and antiplasmodial properties as they have been described to inhibit the development of parasites responsible for malaria. Scorpine-like peptides are composed of two structural domains: one α-helical N-terminal domain, and a C-terminal domain with the cysteine-stabilized α/β motif, which confers the peptide the function of blocking potassium channels and/or anti-bacteria activity. In this work, two C-terminal domains from Scorpine-like peptides were constructed and expressed in Escherichia coli, and their function was analyzed. We were able to demonstrate that the recombinant C-terminal domains rCterVm and rCterHg showed antiplasmodial activity producing 60% and 90% inhibition, respectively, of Plasmodium berghei development at 1 µM and 0.15 µM concentration, which makes these peptides promising candidates against Malaria.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6

Similar content being viewed by others

Data Availability

All data and material are included in Materials and Methods section.

References

Download references

Acknowledgements

Leonel Vargas-Jaimes is a doctoral student from the Programa de Doctorado en Ciencias Biomédicas, Universidad Nacional Autónoma de México (UNAM) and received the fellowship 287191 from Consejo Nacional de Ciencia y Tecnología (CONACyT). This work was partially supported by grant IN202619 from Dirección General de Personal Académico, UNAM of Dr. Lourival D. Possani. The authors acknowledge assistance of Dr. Fernando Zamudio for the determination of molecular mass by spectrometry, and amino acid sequence by Edman degradation.

Funding

This work was partially supported by grant IN202619 from Dirección General de Personal Académico, Universidad Nacional Autónoma de México (UNAM) of Dr. Lourival D. Possani. Leonel Vargas-Jaimes received the fellowship 287191 from Consejo Nacional de Ciencia y Tecnología (CONACyT).

Author information

Authors and Affiliations

Authors

Contributions

All authors contributed significantly to performance of the experiments, conceived the idea, supervised the project, and wrote the manuscript.

Corresponding author

Correspondence to Verónica Quintero-Hernández.

Ethics declarations

Conflict of interest

The authors have declared that no competing interests exist.

Consent to Participate

All the authors have declared their consent to participate in this article.

Consent for Publication

All the authors have declared their consent to publish this article.

Ethical Approval

This article does not contain any studies with human participants or animal performed by any of the authors.

Additional information

Publisher’s Note

Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Rights and permissions

Reprints and permissions

About this article

Check for updates. Verify currency and authenticity via CrossMark

Cite this article

Vargas-Jaimes, L., Rodriguez, M.C., Argotte-Ramos, R. et al. Recombinant C-Terminal Domains from Scorpine-like Peptides Inhibit the Plasmodium berghei Ookinete Development In Vitro. Int J Pept Res Ther 27, 817–829 (2021). https://doi.org/10.1007/s10989-020-10130-7

Download citation

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10989-020-10130-7

Keywords

Navigation