Opposed Aromatic Surfaces Behave as Independent Binding Sites for Carbohydrate Stacking: Analysis of Sandwich-like CH/π/CH Complexes.

CH/π bonds are versatile elements for the construction of complex molecular architectures, thus playing key roles in many biomolecular recognition processes. Although seldom acknowledged, aromatic units are inherently bivalent and can participate in CH/π bonds through either face simultaneously, leading to the formation of stacking complexes. This sandwich-like arrangement is by far the most common in natural complexes and could potentially lead to negative cooperativity due to unfavorable polarization or electrostatic effects, especially when polarized CH fragments are involved.

Illuminating a Solvent-Dependent Hierarchy for Aromatic CH/π Complexes with Dynamic Covalent Glyco-Balances.

CH/π interactions are prevalent among aromatic complexes and represent invaluable tools for stabilizing well-defined molecular architectures. Their energy contributions are exceptionally sensitive to various structural and environmental factors, resulting in a context-dependent nature that has led to conflicting findings in the scientific literature. Consequently, a universally accepted hierarchy for aromatic CH/π interactions has remained elusive.

SARS-CoV-2 S protein activates NLRP3 inflammasome and deregulates coagulation factors in endothelial and immune cells.

Background: Hyperinflammation, hypercoagulation and endothelial injury are major findings in acute and post-COVID-19. The SARS-CoV-2 S protein has been detected as an isolated element in human tissues reservoirs and is the main product of mRNA COVID-19 vaccines. We investigated whether the S protein alone triggers pro-inflammatory and pro-coagulant responses in primary cultures of two cell types deeply affected by SARS-CoV-2, such are monocytes and endothelial cells.