A Short Peptide That Mimics the Binding Domain of TGF-β1 Presents Potent Anti-Inflammatory Activity

作者: Emília R. Vaz , Patrícia T. Fujimura , Galber R. Araujo , Carlos A. T. da Silva , Rangel L. Silva

DOI: 10.1371/JOURNAL.PONE.0136116

关键词:

摘要: The transforming growth factor beta 1 (TGF-β1) is a pleiotropic cytokine with multiple roles in development, wound healing, and immune regulation. TGF-β1-mediated dysfunction may lead to pathological conditions, such as inflammation. Chronic inflammatory process characterized by continuous release of pro-inflammatory cytokines, the inhibition or blockage these cytokines signaling pathways are considered target treatment. In this context, despite high numbers TGF-β-targeted pathways, inducible regulatory T cells (iTreg) control inflammation seems be promising approach. Our aim was develop novel peptides through phage display (PhD) technology that could mimic TGF-β1 function higher potency. Specific mimetic were obtained PhD subtraction strategy from whole cell binding using recombinant competitor during elution step. We have selected peptide play an important role on cellular differentiation modulation TNF-α IL-10 cytokines. synthetic pm26TGF-β1 tested PBMC significantly down-modulated up-regulated responses, leading (Treg) phenotype differentiation. Furthermore, able decrease leukocytes rolling BALB/C mice neutrophils migration C57BL/6 mice. These data suggest useful for treatment diseases, especially because it displays potent anti-inflammatory properties do not exhibit neutrophils’ chemoattraction.

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