De novo design of helical peptides to inhibit tumor necrosis factor-α by disrupting its trimer formation

MedChemComm ◽  
2016 ◽  
Vol 7 (4) ◽  
pp. 725-729 ◽  
Author(s):  
Qi Shen ◽  
Changsheng Zhang ◽  
Hongbo Liu ◽  
Yuting Liu ◽  
Junyue Cao ◽  
...  
Keyword(s):  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
De Novo ◽  
De Novo Design ◽  
Helical Peptide ◽  
Tnfα Inhibitors ◽  
Trimer Formation ◽  
Factor Α ◽  
Necrosis Factor ◽  
Inhibit Tumor Necrosis Factor

Helical peptide TNFα inhibitors were designed by targeting their dimer structure.

scholarly journals Tumor necrosis factor-α (TNFα) inhibitors in the treatment of nonradiographic axial spondyloarthritis: current evidence and place in therapy

2017 ◽  
Vol 9 (8) ◽  
pp. 197-210 ◽  
Author(s):  
Valeria Rios Rodriguez ◽  
Denis Poddubnyy
Keyword(s):  
Ankylosing Spondylitis ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Axial Spondyloarthritis ◽  
Efficacy And Safety ◽  
Tnfα Inhibitors ◽  
Factor Α ◽  
Nonradiographic Axial Spondyloarthritis ◽  
Necrosis Factor

Nonradiographic axial spondyloarthritis (SpA) and radiographic SpA (also known as ankylosing spondylitis) are currently considered as two stages or forms of one disease (axial SpA). The treatment with tumor necrosis factor-α (TNFα) inhibitors has been authorized for years for ankylosing spondylitis. In recent years, most of the anti-TNFα agents have also been approved for the treatment of nonradiographic axial SpA by the European Medicines Agency (EMA) and similar authorities in many countries around the world (but not in the US), increasing the number of possible therapies for this indication. Data from several clinical trials have demonstrated the good efficacy and safety profiles from those anti-TNFα agents. Presently, a large number of patients achieve a satisfactory clinical control with the current therapies, however, there remains a percentage refractory to nonsteroidal anti-inflammatory drugs (NSAIDs) and TNFα inhibitors; therefore, several new drugs are currently under investigation. In 2015, the first representative of a new class of biologics [an interleukin (IL)-17 inhibitor] secukinumab, was approved for the treatment of ankylosing spondylitis; a clinical trial in nonradiographic axial SpA is currently underway. In this review, we discuss the recent data on efficacy and safety of TNFα-inhibitors focusing on the treatment of nonradiographic axial SpA.

scholarly journals Mycobacterium marinumLipooligosaccharides Are Unique Caryophyllose-containing Cell Wall Glycolipids That Inhibit Tumor Necrosis Factor-α Secretion in Macrophages

2009 ◽  
Vol 284 (31) ◽  
pp. 20975-20988 ◽  
Author(s):  
Yoann Rombouts ◽  
Adeline Burguière ◽  
Emmanuel Maes ◽  
Bernadette Coddeville ◽  
Elisabeth Elass ◽  
...  
Keyword(s):  
Cell Wall ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor ◽  
Inhibit Tumor Necrosis Factor

Secoisolariciresinol and isotaxiresinol inhibit tumor necrosis factor-α-dependent hepatic apoptosis in mice

Life Sciences ◽  
2004 ◽  
Vol 74 (22) ◽  
pp. 2781-2792 ◽  
Author(s):  
Arjun H Banskota ◽  
Nhan Trung Nguyen ◽  
Yasuhiro Tezuka ◽  
Quan Le Tran ◽  
Takahiro Nobukawa ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Factor Α ◽  
Necrosis Factor ◽  
Inhibit Tumor Necrosis Factor

Iridium complexes inhibit tumor necrosis factor-α by utilizing light and mixed ligands

2016 ◽  
Vol 808 ◽  
pp. 122-127 ◽  
Author(s):  
Elodie Sauvageot ◽  
Pierre Lafite ◽  
Eric Duverger ◽  
Ronan Marion ◽  
Matthieu Hamel ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Iridium Complexes ◽  
Mixed Ligands ◽  
Factor Α ◽  
Necrosis Factor ◽  
Inhibit Tumor Necrosis Factor

Lactoferrin: influences on Langerhans cells, epidermal cytokines, and cutaneous inflammation

2002 ◽  
Vol 80 (1) ◽  
pp. 103-107 ◽  
Author(s):  
I Kimber ◽  
M Cumberbatch ◽  
R J Dearman ◽  
D R Headon ◽  
M Bhushan ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Langerhans Cells ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
De Novo ◽  
Intradermal Injection ◽  
Interleukin 1Β ◽  
Tnf Α ◽  
Factor Α ◽  
Necrosis Factor

It has been suggested previously that, in addition to other biological roles, lactoferrin (LF) may display anti-inflammatory properties secondary to the regulation of cytokine expression. To explore this concept further, we have here examined in human volunteers the influence of recombinant homologous LF on the migration of epidermal Langerhans cells (LC), a process that is known to be dependent upon the local availability of certain proinflammatory cytokines including tumor necrosis factor α (TNF-α) and interleukin 1β (IL-1β). In common with previous studies in mice, it was found that topical administration of LF prior to exposure at the same site to the contact sensitizer diphenylcyclopropenone resulted in a significant reduction of allergen-induced LC migration from the epidermis (measured as a function of the frequency of CD1a+ or HLA-DR+ LC found in epidermal sheets prepared from punch biopsies of the treated skin sites). However, under the same conditions of exposure, LF was unable to influence migration of LC induced by the intradermal administration of TNF-α data consistent with the hypothesis that one action of LF in the skin is to regulate the local production of this cytokine. Further support for this hypothesis was derived from experiments conducted with IL-1β. This cytokine is also able to induce the mobilization of LC following intradermal injection, although in this case, migration is known to be dependent upon the de novo production of TNF-α. We observed that prior exposure to LF resulted in a substantial inhibition of IL-1β-induced LC migration, data again consistent with the regulation of TNF-α production by LF. Collectively, these results support the view that LF is able to influence cutaneous immune and inflammatory processes secondary to regulation of the production of TNF-α and possibly other cytokines.Key words: lactoferrin, Langerhans cells, tumor necrosis factor α, interleukin 1β.

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