| Summary: | 碩士 === 國立清華大學 === 生物科技研究所 === 101 === In America, there are about 750,000 cases of septic shock each year. Among these cases, 225,000 of them are fatal. The major cause of sepsis is from endotoxin (also referred as lipopolysaccharide or LPS). Endotoxin constitutes the major component of the outer leaflet of Gram-negative bacteria membrane and is released to blood or tissue upon lysis of bacteria. While structure-activity relationships have been extensively studied with regard to antimicrobial peptide and bacteria membrane interactions, less is known about the anti-endotoxin effects of antimicrobial peptides.
Previously, we have developed an easy strategy to boost salt resistance and serum stability of short antimicrobial peptides by adding the non-nature bulky amino acid β-naphthylalanine to their C-termini. The activities of the short salt-sensitive tryptophan-rich peptide S1 were diminished at high salt concentrations, whereas the activities of its β-naphthylalanine end-tagged variants were less affected. β-naphthylalanine end-tagging may help these peptides to penetrate deeper into the bacterial and fungal cell membranes, hence making these peptides more efficient at disrupting the membranes even under high salt conditions. Herein, we have extended this study to characterize the anti-endotoxin effects of β-naphthylalanine end-tagged short antimicrobial peptides. The results will be used to help us design more clinical feasible antimicrobial peptides.
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