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Structure of a Synthetic Fragment of the Lipopolysaccharide (LPS) Binding Protein When Bound to LPS and Design of a Peptidic LPS Inhibitor

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journal contribution
posted on 01.12.2005, 00:00 authored by Primož Pristovšek, Saša Simčič, Branka Wraber, Uroš Urleb
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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