Abstract
Laccase from pathogenic fungi participates in both the delignification and neutralization of phytoantibiotics. Furthermore, it interferes with the hormone signaling in plants and catalyzes melanization. Infections of these pathogens contribute to loss in forestry, agriculture, and horticulture. As there is still a need to expand knowledge on efficient defense strategies against phytopathogenic fungi, the present study aimed to reveal more information on the molecular mechanisms of laccase inhibition with natural and natural-like carboxylic acid semi-synthetic derivatives. A set of hydrazide-hydrazones derived from carboxylic acids, generally including electron-rich arene units that serve as a decoy substrate, was synthesized and tested with laccase from Trametes versicolor. The classic synthesis of the title inhibitors proceeded with good to almost quantitative yield. Ninety percent of the tested molecules were active in the range of KI = 8–233 µM and showed different types of action. Such magnitude of inhibition constants qualified the hydrazide-hydrazones as strong laccase inhibitors. Molecular docking studies supporting the experimental data explained the selected derivatives’ interactions with the enzyme. The results are promising in developing new potential antifungal agents mitigating the damage scale in the plant cultivation, gardening, and horticulture sectors.
Highlights
IntroductionLaccase (benzenediol: oxygen oxidoreductase, EC 1.10.3.2) is a blue multi-copper oxidase specific to a broad group of electron-rich arenes such as anilines and phenols
Laccase is a blue multi-copper oxidase specific to a broad group of electron-rich arenes such as anilines and phenols
The target products were synthesized in a three-step procedure starting from carboxylic acid 1 via
Summary
Laccase (benzenediol: oxygen oxidoreductase, EC 1.10.3.2) is a blue multi-copper oxidase specific to a broad group of electron-rich arenes such as anilines and phenols. It has the exceptional ability to one electron oxidize both low- and high-molecular-weight substrates via direct or mediated reactions applied in green chemistry [1]. Laccase participates in fungal metabolic pathways such as developing fruit bodies, the pigmentation of spores, and sexual differentiation [9]. It is known as the virulence factor involved in the pathogenicity of humans [10,11,12] and plants [13,14,15,16]. Fungi release laccase into the plant tissues It catalyzes lignin decomposition and neutralization of the auxins and phytoalexins, a primary barrier against pathogen attack.
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call
