Endotoxinbinding

Endotoxinbinding refers to the interaction between endotoxins, primarily lipopolysaccharide (LPS) molecules from the outer membrane of Gram-negative bacteria, and other molecules that bind endotoxin to neutralize, detoxify, or remove it from biological systems. Binding can influence how endotoxin is distributed, sensed by the immune system, and cleared from the body, and it can occur in physiological contexts as well as in engineered or therapeutic settings.

In humans, several endogenous proteins bind LPS with varying effects on toxicity and signaling. Lipopolysaccharide-binding protein (LBP) binds circulating LPS and presents it to the CD14/TLR4/MD-2 receptor complex, aiding innate immune sensing. Bactericidal permeability-increasing protein (BPI) binds LPS with high affinity and can counteract some endotoxic activities. The coordinated action of these and related molecules modulates inflammatory responses and endotoxin clearance.

Therapeutic and research applications employ exogenous endotoxin binders to neutralize and remove LPS. Polymyxin B and its derivatives have a high affinity for lipid A, enabling binding-based removal of endotoxin in affinity columns or hemoperfusion devices, though their clinical use is limited by toxicity. Endotoxin-binding resins, charcoal, and various synthetic polymers are used to adsorb LPS in laboratory settings and certain extracorporeal treatments. Antibodies against LPS and engineered binding peptides are also explored as strategies to prevent or dampen endotoxin-triggered inflammation.

Endotoxinbinding is a significant topic in sepsis research, diagnostics, and blood purification. Its effectiveness depends on binding strength, accessibility of endotoxin, and the clinical context, while safety and specificity remain critical considerations for practical applications.