Bactericidal and endotoxin neutralizing activity of a peptide derived from Limulus antilipopolysaccharide factor

Identification, cloning, characterization and recombinant expression of an anti-lipopolysaccharide factor from the hemocytes of Indian mud crab, Scylla serrata

“…These observations concur with earlier reports by Warren et al have demonstrated the ability of LALF to neutralize LPS derived from many different species of gram negative organisms because of its affinity for the toxic lipid A moiety of LPS [37]. Weiss and colleagues [34] have described the LPS neutralizing activity of a synthetic peptide derived from the active domain of LALF (LALF #28-54).…”

“…The results summarized in Table 2 clearly indicate a stronger inhibition of growth in Gram-negative bacteria than observed in Gram-positive bacteria. Such a finding could be attributed to the presence of LPS in gram negative bacteria, which has been demonstrated to be the binding target of ALF, as reported earlier [34].…”

“…This crystal structure was used to design synthetic peptides based on the proposed endotoxin-binding domain of rLALF [10]. While most of the peptides were studied for their endotoxin-binding and neutralizing activities, others demonstrated bactericidal activities against P. aeruginosa and inhibited LPS-induced tumor necrosis factor-alpha secretion [34,35]. Somboonwiwat and colleagues [6] have prepared a recombinant form of ALFPm3 from the black tiger shrimp P. monodon, using a Pichia pastoris system.…”

Bactericidal and Antiendotoxic Properties of Short Cationic Peptides Derived from a Snake Venom Lys49 Phospholipase A2

“…Whereas the former decreased the rate of LPS-induced mortality by 40% (concomitantly with a significant reduction in the levels of TNF-␣ in serum), no significant differences in lethality or in TNF-␣ concentrations were observed in pEM-2 (L)-treated mice. These results suggest that pEM-2 (L) might be rapidly eliminated by proteolysis or renal clearance, similar to other small cationic L-peptides (2,6,35,38), whereas the half-life of pEM-2 (D) might be more prolonged in vivo.…”

The Sushi peptides: structural characterization and mode of action against Gram-negative bacteria

“…The CAP18-derived peptide contains 37 amino acids of the C-terminal LPS-binding domain of rabbit CAP18 protein, which was found to harbor antibacterial activity against various Gram-negative and Grampositive bacteria [76]. Another peptide derived from the active domain of LALF [27, 29 -54] was also found to exhibit antimicrobial activity similar to that of Review Article LALF itself and could potentially be useful as a therapeutic agent [77]. These peptides, derived from parts of LBPs with or without modification, have been analyzed for their high antimicrobial potency.…”