In Vitro and Computational Response of Differential Catalysis by BAFC 633 Laccase in Interaction with 2,4-D and Chlorpyrifos.

Enzymes secreted by white rot fungi (WRF), such as laccase, offer a promising approach for the treatment of hazardous xenobiotic compounds. This study conducted a comprehensive analysis of the impact of the pesticides 2,4-dichlorophenoxyacetic acid (2,4-D) and chlorpyrifos on the laccase of BAFC 633 through in vitro and bioinformatics analyses. The fungal strain was shown to be tolerant to both pesticides, with notable morphological and ultrastructural alterations in the mycelium.

Catalytic function of the laccase enzyme in response to chlorpyrifos and 2,4-dichlorophenoxyacetic acid: behavior in controlled and simulated environments.

Enzymes secreted by white-rot fungi, such as laccase, offer a promising solution for treating xenobiotic compounds dangerous to the environment and human health. This study aimed to perform a comprehensive analysis of the tolerance of Pleurotus pulmonarius LBM 105 and its laccase activity toward the pesticides 2,4-D and chlorpyrifos both in vitro and in silico. The fungal strain was able to grow in different concentrations of the pesticides, showing evident morphological alterations.

Unveiling crucial amino acids in the carbohydrate recognition domain of a viral protein through a structural bioinformatic approach.

Carbohydrate binding modules (CBMs) are protein domains that typically reside near catalytic domains, increasing substrate-protein proximity by constraining the conformational space of carbohydrates. Due to the flexibility and variability of glycans, the molecular details of how these protein regions recognize their target molecules are not always fully understood. Computational methods, including molecular docking and molecular dynamics simulations, have been employed to investigate lectin-carbohydrate interactions.

An efficient use of X-ray information, homology modeling, molecular dynamics and knowledge-based docking techniques to predict protein-monosaccharide complexes.

Unraveling the structure of lectin-carbohydrate complexes is vital for understanding key biological recognition processes and development of glycomimetic drugs. Molecular Docking application to predict them is challenging due to their low affinity, hydrophilic nature and ligand conformational diversity. In the last decade several strategies, such as the inclusion of glycan conformation specific scoring functions or our developed solvent-site biased method, have improved carbohydrate docking performance but significant challenges remain, in particular, those related to receptor conformational diversity.