Lipopolysaccaride-binding peptides obtained by phage display method.

Authors :: Matsumoto M
Horiuchi Y
Yamamoto A
Ochiai M
Niwa M
Takagi T
Omi H
Kobayashi T
Suzuki MM
Source :: Journal of microbiological methods [J Microbiol Methods] 2010 Jul; Vol. 82 (1), pp. 54-8. Date of Electronic Publication: 2010 Apr 20.
Publication Year :: 2010
Abstract: Lipopolysaccharide (LPS) is a major component of the outer membrane of Gram-negative bacteria. It has strong toxicity and might cause sepsis or septic shock. Thus early detection of LPS and neutralization of LPS toxicity are required. We obtained several new LPS-binding peptides using a phage display method. We synthesized 3 of these peptides and analyzed their binding affinity and capacity to LPS. One of these peptides, named Li5-001, showed high binding affinity to LPS and lipid A; the K(d) values were 10 and 1 nM, respectively. Li5-001 showed a high binding capacity to LPS, and was estimated to bind 130 ng LPS/mg, which is higher than that of polymyxin B (80 ng LPS/mg); however, its LPS-neutralizing activity was low. Li5-001 coupled with beads will be useful for eliminating endotoxin contamination from pharmaceuticals. Its low LPS-neutralizing activity allows to be used in the Limulus amebocyte lysate test without eluting LPS from the Li5-001 coupled beads.<br /> (Copyright (c) 2010 Elsevier B.V. All rights reserved.)