Amphiphilicity-Driven Small Alcohols Regulate the Flexibility of Pesticide-Loaded Microcapsules for Better Foliar Adhesion and Utilization.

The foliar loss of pesticides causes serious utilization decline and environmental risk. On the basis of biomimetics, pesticide-loaded microcapsules (MCs) with spontaneous deformation on foliar micro/nanostructures, like the snail suction cup, are prepared by interfacial polymerization. By controlling the usage or types of small alcohols in the MC preparation system, the flexibility of MCs is tunable. Through the investigation of emulsions and MC structures, we discover that the migration and distribution of small alcohols driven by amphiphilicity affect the process of interfacial polymerization between polyethylene glycol and 4,4-methylenediphenyl diisocyanate. By hydrophobic modification of the polymer and competition for oil monomers of small alcohols, the thickness and compactness of shells are reduced, whereas the density of the core is increased. As a result of the regulation in structures, the flexibility of MCs is improved significantly. In particularly, the MCs-N-pentanol (0.1 mol kg-1) with the best flexibility show strong scouring resistance on varied foliar structures, sustained release property on the air/solid interface, and persistent control effect against foliar diseases. The pesticide-loaded soft MCs provide an effective way to improve pesticide foliar utilization.

Efficient screening of protein-ligand complexes in lipid bilayers using LoCoMock score.

Membrane proteins are attractive targets for drug discovery due to their crucial roles in various biological processes. Studying the binding poses of amphipathic molecules to membrane proteins is essential for understanding the functions of membrane proteins and docking simulations can facilitate the screening of protein-ligand complexes at low computational costs. However, identifying docking poses for a ligand in non-aqueous environments such as lipid bilayers can be challenging. To address this issue, we propose a new docking score called logP-corrected membrane docking (LoCoMock) score. To screen putative protein-ligand complexes embedded in a membrane, the LoCoMock score considers the affinity between a target ligand and the membrane. It combines the docking score of the protein-ligand complex with the logP of the target ligand. In demonstrations using several model ligands, the LoCoMock score screened more putative complexes than the conventional docking score. As extended docking, the LoCoMock score makes it possible to screen membrane proteins more effectively as drug targets than the conventional docking.