Abstract
Arthropoda is a phylum of invertebrates that has undergone remarkable evolutionary radiation, with a wide range of venomous animals. Arthropod venom is a complex mixture of molecules and a source of new compounds, including antimicrobial peptides (AMPs). Most AMPs affect membrane integrity and produce lethal pores in microorganisms, including protozoan pathogens, whereas others act on internal targets or by modulation of the host immune system. Protozoan parasites cause some serious life-threatening diseases among millions of people worldwide, mostly affecting the poorest in developing tropical regions. Humans can be infected with protozoan parasites belonging to the genera Trypanosoma, Leishmania, Plasmodium, and Toxoplasma, responsible for Chagas disease, human African trypanosomiasis, leishmaniasis, malaria, and toxoplasmosis. There is not yet any cure or vaccine for these illnesses, and the current antiprotozoal chemotherapeutic compounds are inefficient and toxic and have been in clinical use for decades, which increases drug resistance. In this review, we will present an overview of AMPs, the diverse modes of action of AMPs on protozoan targets, and the prospection of novel AMPs isolated from venomous arthropods with the potential to become novel clinical agents to treat protozoan-borne diseases.
Highlights
Arthropoda is a phylum of invertebrate animals that have a rigid exoskeleton with several pairs of articulated appendages whose number varies according to the class [1]
Leishmaniasis is a vector-borne disease that is caused by obligate intracellular protozoan of the Leishmania genus [172,173]
There are five possible protozoa that may be related to malaria, all belonging to the Plasmodium genus: P. vivax, P. falciparum, P. malariae, P. ovale, and P. knowlesi [201]
Summary
Arthropoda is a phylum of invertebrate animals that have a rigid exoskeleton with several pairs of articulated appendages whose number varies according to the class [1]. AMPs are usually small molecules (~10–50 residues long), gene-encoded, cationic, and amphipathic, with a miscellaneous composition of amino acids [40,41,42,43] Despite their vast structural diversity, most AMPs kill pathogens microorganisms through membrane damage, protecting the host from bacteria, viruses, fungi, and parasites [44,45,46]. Β-sheet peptides are a diverse group of molecules, containing six to eight cysteine residues, responsible for formation of two or more disulfide bonds that will stabilize the β-sheet structure They present a well-defined number of β-strands, amphipathically organized, with distinguishable hydrophobic and hydrophilic surfaces [62,63,64]. Additional efforts are necessary to extend these findings in the path to drug development and to prospect further the antiparasitic potential of AMPs from animal venoms
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