The conserved N-terminal histidine in an engineered peptide mediates sepsis treatment efficacy via dual binding to CD14 and LPS
Sepsis remains a major clinical challenge due to the limited efficacy of existing therapies in controlling excessive inflammation. The engineered stapled peptide sHVF18, derived from an evolutionarily conserved thrombin innate fold, binds both lipopolysaccharide (LPS) and the LPS-binding groove of CD14, enabling dual targeting of bacterial components and host immune signaling. To define structural
