Oligomeric Protein LPS Binding via Coiled-Coil Structure

The patent changes the binding affinity parameter by using an oligomeric protein with a coiled-coil structure that provides nanomolar binding affinity, significantly improving upon the micromolar range of polymyxin B while maintaining specificity through the structured interaction with lipid A

The patent applies local quality by creating a specific binding interface through the coiled-coil structure that interacts selectively with the lipid A component of LPS, rather than using non-specific electrostatic interactions like poly-lysine. The structured helical arrangement provides localized specific binding sites that avoid non-specific interactions with other negatively charged molecules

The patent uses an intermediary approach by employing the oligomeric protein as a selective mediator that binds LPS through specific structural interactions with lipid A, rather than relying on non-specific electrostatic interactions. This intermediary protein provides selective binding that is not competed by other charged particles in the sample

The patent applies copying by creating a simplified, sustainable alternative to the complex LAL assay system. Instead of using expensive horseshoe crab amebocyte lysate, the patent uses a recombinant oligomeric protein that can be produced in bacterial expression systems, providing the same detection capability at lower cost and with better sustainability