2. Academic Validation
  3. Structure of a synthetic fragment of the lipopolysaccharide (LPS) binding protein when bound to LPS and design of a peptidic LPS inhibitor

Structure of a synthetic fragment of the lipopolysaccharide (LPS) binding protein when bound to LPS and design of a peptidic LPS inhibitor

  • J Med Chem. 2005 Dec 1;48(24):7911-4. doi: 10.1021/jm050762a.
Primoz Pristovsek 1,  Sasa Simcic,  Branka Wraber,  Uros Urleb
Affiliations

Affiliation

  • 1 Laboratory of Biotechnology, National Institute of Chemistry, Hajdrihova 19, 1000 Ljubljana, Slovenia. primoz.pristovsek@ki.si
PMID: 16302828 DOI: 10.1021/jm050762a
Abstract

Peptidic lipopolysaccharide (LPS) antagonists are the subject of intensive research. We report an NMR and modeling study of LBP-14 (RVQGRWKVRASFFK), a synthetic fragment of the LPS binding protein (LBP). In a mixture with LPS we observed the transferred nuclear Overhauser effect and determined the LPS-bound structure of LBP-14 that was used for docking calculations to LPS. The derived complex was used to design a peptide that displayed more than 50% increase in LPS inhibition in vitro.

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