1. An MD2 Hot-Spot-Mimicking Peptide that Suppresses TLR4-Mediated Inflammatory Response in vitro and in vivo
- Author
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Peter F. Slivka, Hang Yin, Zeno Fiorini, Mark R. Hutchinson, Liping Liu, Nilanjan Ghosh, and Linda R. Watkins
- Subjects
Azoles ,Lipopolysaccharides ,Peptidomimetic ,Molecular Sequence Data ,Lymphocyte Antigen 96 ,T-Cell Antigen Receptor Specificity ,Peptide ,Molecular Dynamics Simulation ,Biology ,medicine.disease_cause ,Biochemistry ,Article ,Cell Line ,Mice ,In vivo ,medicine ,Animals ,Humans ,Pain Management ,Amino Acid Sequence ,Molecular Biology ,Peptide sequence ,Nitrobenzenes ,Inflammation ,chemistry.chemical_classification ,Macrophages ,Molecular Mimicry ,Organic Chemistry ,Molecular biology ,Peptide Fragments ,In vitro ,Rats ,Cell biology ,Toll-Like Receptor 4 ,Molecular mimicry ,Spectrometry, Fluorescence ,chemistry ,Cell culture ,Neuralgia ,Molecular Medicine ,Neuroglia ,Protein Binding - Abstract
A truncated peptide was shown to retain the structure of the TLR4-binding hot-spot region of MD2, disrupting with the TLR4/MD2 interactions. The peptide not only demonstrated strong binding affinity in the fluorescence polarization assay, but also showed high specificity in macrophage cells. Furthermore, MD2-I was able to suppress neuropathic pain in animal models.
- Published
- 2011
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