M. Kloczewiak et al., SYNTHETIC PEPTIDES THAT MIMIC THE BINDING-SITE OF HORSESHOE-CRAB ANTILIPOPOLYSACCHARIDE FACTOR, The Journal of infectious diseases, 170(6), 1994, pp. 1490-1497
Tachypleus antilipopolysaccharide (LPS) factor (TALF) is a protein of
102 amino acids in the lysate of amebocytes of Tachypleus tridentatus
that binds bacterial LPS with high affinity and blocks its biologic ac
tivity in numerous assays. To elucidate the minimal sequences that bin
d LPS, overlapping synthetic peptides based on the sequence of TALF we
re assessed for the ability to bind and neutralize LPS. TALF41-53 was
the minimal sequence that bound LPS, as assessed by a slot blot captur
e assay. TALF29-59 bound LPS with the highest potency. TALF29-59 decre
ased LPS-induced coagulation of limulus amebocyte lysate, induction of
cytokines from human monocytes, and LPS-induced lethality in sensitiz
ed mice. Synthetic peptides based on TALF or other LPS-binding protein
s may be useful for the design of drugs for treatment of endotoxemia.