Design of a Repellent Against Aedes aegypti (Diptera: Culicidae) Using in silico Simulations With AaegOBP1 Protein.

Skin irritation has been reported to be the main adverse effect of excessive use of N,N-diethyl-m-toluamide (DEET) and ethyl 3-acetyl(butyl)amino (IR3535) commercial repellents. Therefore, there is an interest in alternatives of natural origin such as essential oils (EOs) and major compounds, which have repellent effects but have no contraindications. The main purpose of the present study was to identify the repellent effect of selected terpenes on Aedes aegypti Linnaeus, 1762 (Diptera: Culicidae) by in silico analysis based on their affinity with the odorant protein AaegOBP1.

Synthesis, Biological Evaluation and In Silico Computational Studies of 7-Chloro-4-(1-1,2,3-triazol-1-yl)quinoline Derivatives: Search for New Controlling Agents against (Lepidoptera: Noctuidae) Larvae.

The insecticidal and antifeedant activities of five 7-chloro-4-(1-1,2,3-triazol-1-yl)quinoline derivatives were evaluated against the maize armyworm, (J.E. Smith).

Structural insights into the pre-amyloid tetramer of β-2-microglobulin from covalent labeling and mass spectrometry.

The main pathogenic process underlying dialysis-related amyloidosis is the accumulation of β-2-microglobulin (β2m) as amyloid fibrils in the musculoskeletal system, and some evidence suggests that Cu(II) may play a role in β2m amyloid formation. Cu(II)-induced β2m fibril formation is preceded by the formation of discrete, oligomeric intermediates, including dimers, tetramers, and hexamers. In this work, we use selective covalent labeling reactions combined with mass spectrometry to investigate the amino acids responsible for mediating tetramer formation in wild-type β2m.

Structure of the preamyloid dimer of beta-2-microglobulin from covalent labeling and mass spectrometry.

Beta-2-microglobulin (beta2m) self-associates into fibrillar amyloid deposits in the musculoskeletal system of patients undergoing hemodialysis treatment. Previous studies have shown that stoichiometric amounts of Cu(II) at near physiological conditions can cause beta2m to organize into native-like dimers prior to forming amyloid fibrils. Here, we report the results from selective covalent labeling reactions combined with mass spectrometry that provide insight into the amino acid residues that mediate dimer formation in the wild-type protein.