Abstract
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) do not have a stable 3D structure but still have important biological activities. Jaburetox is a recombinant peptide derived from the jack bean (Canavalia ensiformis) urease and presents entomotoxic and antimicrobial actions. The structure of Jaburetox was elucidated using nuclear magnetic resonance which reveals it is an IDP with small amounts of secondary structure. Different approaches have demonstrated that Jaburetox acquires certain folding upon interaction with lipid membranes, a characteristic commonly found in other IDPs and usually important for their biological functions. Soyuretox, a recombinant peptide derived from the soybean (Glycine max) ubiquitous urease and homologous to Jaburetox, was also characterized for its biological activities and structural properties. Soyuretox is also an IDP, presenting more secondary structure in comparison with Jaburetox and similar entomotoxic and fungitoxic effects. Moreover, Soyuretox was found to be nontoxic to zebra fish, while Jaburetox was innocuous to mice and rats. This profile of toxicity affecting detrimental species without damaging mammals or the environment qualified them to be used in biotechnological applications. Both peptides were employed to develop transgenic crops and these plants were active against insects and nematodes, unveiling their immense potentiality for field applications.
Highlights
Disordered proteins (IDPs) and intrinsically disordered regions (IDRs) fail to form a stable tridimensional structure, challenging the century-old paradigm that a biological function is a specific property of a unique structure
Similar results were obtained in the central nervous system of the related triatome R. prolixus, with both in vivo and in vitro Jaburetox treatments leading to a decrease in nitric oxide synthase (NOS) enzyme activity without affecting its gene expression
The profile of UDP-N-acetylglucosamine pyrophosphorylase (UAP) modulation by the Jaburetox in N. cinerea was different, since its activity was only affected 18 h after injection. This distinct response when compared to the triatomines could be related to the fact that this cockroach is so far the only species found to be resistant to the acute lethal effect of Jaburetox [86]
Summary
Disordered proteins (IDPs) and intrinsically disordered regions (IDRs) fail to form a stable tridimensional structure, challenging the century-old paradigm that a biological function is a specific property of a unique structure. A typical IDP/IDR has a multitude of elements for potentially foldable, partially foldable, differently foldable, or unfoldable protein segments [5,6]. Their folding can be acquired after the interaction with proteins, nucleic acids, membranes, or small molecules. These conformation modifications can be driven by changes in the IDPs environment as well as post-translational modifications. NMR can provide data about mobility of the unstructured regions [4,11] In this way, NMR is possibly the most powerful technique for structural studies of these disordered proteins [12]. Computational studies assumed an increasingly importance in interpreting these challenging experimental data [11]
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