Structure of a Synthetic Fragment of the LALF Protein When Bound to Lipopolysaccharide
Peptidic lipopolysaccharide (LPS) antagonists are the subject of intensive research. We report an NMR and modeling study of LALF-14 (GCKPTFRRLKWKYKCG), a synthetic cyclized fragment of the limulus anti-LPS factor (LALF) comprising residues 36−47. In a mixture with LPS we observed the transferred NOE...
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Published in | Journal of medicinal chemistry Vol. 48; no. 5; pp. 1666 - 1670 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
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American Chemical Society
10.03.2005
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Abstract | Peptidic lipopolysaccharide (LPS) antagonists are the subject of intensive research. We report an NMR and modeling study of LALF-14 (GCKPTFRRLKWKYKCG), a synthetic cyclized fragment of the limulus anti-LPS factor (LALF) comprising residues 36−47. In a mixture with LPS we observed the transferred NOE effect and derived the LPS-bound structure of LALF-14. Neither the free nor the LPS-bound peptide displays NOEs indicative of a β-sheet-like structure that is adopted by the fragment in the full-size protein. However, docking calculations show that the former structure is not a prerequisite for binding of LALF-14 to LPS. |
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AbstractList | Peptidic lipopolysaccharide (LPS) antagonists are the subject of intensive research. We report an NMR and modeling study of LALF-14 (GCKPTFRRLKWKYKCG), a synthetic cyclized fragment of the limulus anti-LPS factor (LALF) comprising residues 36−47. In a mixture with LPS we observed the transferred NOE effect and derived the LPS-bound structure of LALF-14. Neither the free nor the LPS-bound peptide displays NOEs indicative of a β-sheet-like structure that is adopted by the fragment in the full-size protein. However, docking calculations show that the former structure is not a prerequisite for binding of LALF-14 to LPS. Peptidic lipopolysaccharide (LPS) antagonists are the subject of intensive research. We report an NMR and modeling study of LALF-14 (GCKPTFRRLKWKYKCG), a synthetic cyclized fragment of the limulus anti-LPS factor (LALF) comprising residues 36-47. In a mixture with LPS we observed the transferred NOE effect and derived the LPS-bound structure of LALF-14. Neither the free nor the LPS-bound peptide displays NOEs indicative of a beta-sheet-like structure that is adopted by the fragment in the full-size protein. However, docking calculations show that the former structure is not a prerequisite for binding of LALF-14 to LPS. |
Author | Fehér, Krisztina Pristovšek, Primož Szilágyi, László |
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Keywords | Cyclic peptides Overhauser effect NMR spectrometry Endotoxin Modeling Protein Toxic shock syndrome Infection Toxin Structure activity relation Peptide fragment Sulfur peptide Antiseptic Molecular model Bacteriosis Lipopolysaccharide Staphylococcal infection Conjugated compound Antilipopolysaccharide factor |
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Snippet | Peptidic lipopolysaccharide (LPS) antagonists are the subject of intensive research. We report an NMR and modeling study of LALF-14 (GCKPTFRRLKWKYKCG), a... |
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SubjectTerms | Antibiotics. Antiinfectious agents. Antiparasitic agents Antimicrobial Cationic Peptides Antiseptics Arthropod Proteins Biological and medical sciences Invertebrate Hormones - chemistry Lipopolysaccharides - chemistry Magnetic Resonance Spectroscopy Medical sciences Miscellaneous Models, Molecular Peptide Fragments - chemistry Peptides, Cyclic - chemistry Pharmacology. Drug treatments Protein Binding Solutions Water |
Title | Structure of a Synthetic Fragment of the LALF Protein When Bound to Lipopolysaccharide |
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