Abstract
Bioactive peptides are active against the malaria parasite growth through targeting various stages of life cycle, but their mechanism of action is not fully understood. PFI1625c, a metalloprotease present in Plasmodium falciparum, is a potential drug target, and it shows best binding to peptide P550 (LVIVAKRA). Out of 20 selected antimalarial peptides, 4 peptides namely Dermaseptin S3, Cyclosporin A, Angiotensin II, and PcFK2 show high affinity with PFI1625c. Dermaseptin S3 is making polar contacts and hydrophobic interactions with the residues present within the catalytic site of PFI1625c. The affinity of bioactive peptides toward PFI1625c and anti-malarial activity of peptide shows a strong correlation (R = 0.921), indicating PFI1625c as a potential target behind their antimalarial activity. Thus, current study confirms the involvement of PFI1625c behind the antimalarial activity of tested bioactive peptides, and the result can be helpful to design better bio-compatible antimalarial drugs.
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Acknowledgments
This work was partially supported by the Department of Biotechnology; Govt of India Grants (BT/PR13436/MED/12/450/2009) to V.T. KL acknowledges the financial support in the form of fellowship from Indian Institute of Technology-Guwahati, Assam, India.
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Lhouvum, K., Bhuyar, K.S. & Trivedi, V. Molecular modeling and correlation of PFI1625c-peptide models of bioactive peptides with antimalarial properties. Med Chem Res 24, 1527–1533 (2015). https://doi.org/10.1007/s00044-014-1232-5
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DOI: https://doi.org/10.1007/s00044-014-1232-5