ifn-γ

IFN-γ Antagonist 1 (AYCRDGKIGPPKLDIRKEEKQI), an interferon γ (IFN γ) antagonist, effectively inhibits IFN-γ induced HLR/DR antigen expression in Colon 205 cells, demonstrating an IC50 of approximately 35 μM. This compound shows promise for applications in immune regulation [1].

IFN-γ Antagonist 1 (AYCRDGKIGPPKLDIRKEEKQI) acetate, an interferon γ (IFN γ) antagonist, effectively inhibits the expression of HLR/DR antigen in Colon 205 cells induced by IFN-γ, with an IC50 of approximately 35 μM. This compound holds promise for applications in immune regulation [1].

IFN-α Receptor Recognition Peptide 1, associated with receptor interactions, is a peptide of IFN-α.

Delmitide acetate (RDP58) is an orally active d-isomer decapeptide with potent anti-inflammatory properties, suppressing TNF-α, IFN-γ, and interleukin (IL)-12 production, while enhancing heme oxygenase 1 activity. It is utilized in research related to ulcerative colitis [1] [2].

Delmitide, a TNF-alpha production inhibitor, is used potentially for the treatment of Crohn's disease and ulcerative colitis.

KWAR23 is a monoclonal antibody targeting SIRPα that blocks the interaction of SIRPα and SIRPγ with CD47, impairing chronic T-cell activation and IFN-γ secretion.

MBP (83-99) is an immunodominant epitope recognized by MBP-specific T cell lines, which stimulates both cell proliferation and IFN-γ secretion in T cells [1] [2].

Influenza NP (311-325) is a biologically active peptide consisting of amino acids 311 to 325 from the influenza virus nucleoprotein (NP). As a bona fide MHC class II-restricted epitope, it is critical for studying host immune responses during viral infection, inducing robust gamma interferon (IFN-gamma) production in intracellular cytokine assays without stimulating CD8 T-cells in mice. The presence of Glutamine (Q) or Glutamic acid (E) at the N-terminus can lead to spontaneous formation of Pyroglutamyl (pGlu) peptides, enhancing peptide stability against gastrointestinal proteases. These peptides are considered a normal variant and included in peptide purity measurements in HPLC analysis.

CFP10 (71–85) is an immunologically active peptide that induces IFN-γ production and cytotoxic T lymphocyte (CTL) activity in CD4+ and CD8+ T cells from individuals with diverse MHC class II and I expression profiles.

Interphotoreceptor retinoid-binding protein (1-20) (IRBP1-20), a dodecapeptide fragment of retinoid-binding protein 3, plays a crucial role in pigment regeneration by facilitating the transport of retinol and retinal between photoreceptor cells and the retinal pigment epithelium. It has been utilized to provoke autoimmune uveoretinitis in C57BL/6 mice, possessing the H-2b haplotype. Furthermore, IRBP1-20 at a concentration of 3 µM enhances the secretion of IL-4, IL-5, and IL-6 from primary mouse spleen lymphocytes. Immunization and subsequent rechallenge with IRBP1-20 lead to increased ear swelling, inflammation of ocular blood vessels, infiltration by immune cells, damage to the photoreceptor layer, and retinal detachment in IFN-γ-deficient mice.

Interphotoreceptor retinoid-binding protein (651-670) (IRBP651-670), a peptide fragment of retinoid-binding protein 3 (also known as IRBP), plays a crucial role in the visual cycle by facilitating the transport of retinol and retinal between photoreceptor cells and the retinal pigment epithelium. This transport is essential for the regeneration of pigments necessary for vision. When administered at a dose of 300 µg/animal, IRBP651-670 induces autoimmune uveoretinitis in C57BL/6 mice, a model possessing the H-2b haplotype. This immunization leads to increased levels of ocular cytokines including IL-1β, IL-6, IL-17, TNF-α, and IFN-γ, promotes immune cell infiltration into the eye, and results in photoreceptor cell damage.

TPP-1, a peptide inhibitor, targets the interaction between programmed cell death protein 1 (PD-1) and its ligand (PD-L1), binding specifically to PD-L1 with a dissociation constant (Kd) of 94.67 nM. At a concentration of 20 µM, TPP-1 effectively counteracts the PD-L1-induced suppression of IFN-γ production in anti-CD3-stimulated isolated human CD4+ T cells. Furthermore, TPP-1 demonstrates significant efficacy in reducing tumor volume in a mouse xenograft model of HL-60 leukemia. This model involved HL-60 cells co-cultured with anti-CD3-activated isolated human CD4+ T cells, with TPP-1 administration at a dosage of 4 mg/kg showing notable antitumor activity.

HOXB7 (8-25), a peptide fragment derived from homeobox B7 (HOXB7)—a key controller of cell growth and oncogene activator—facilitates antigen presentation when pulsed onto dendritic cells obtained from human peripheral blood mononuclear cells (PBMCs). This process promotes the activation and interferon-gamma (IFN-γ) production by CD4+ helper T cells, triggering targeted and broad-spectrum antitumor responses.

EGFRvIII peptide, a synthetic peptide mirroring the EGFRvIII fusion junction—a tumor-specific, perpetually active EGFR variant missing amino acids 6-273 of the wild-type—binds to HLA-A*0201-positive T2 cells under MHC class I at 25 µg/ml. It enables antigen presentation in dendritic cells from human peripheral blood mononuclear cells (PBMCs), thus activating CD8+ cytotoxic T lymphocytes and prompting IFN-γ production. Administered at 15 µg/animal with the TLR5 agonist flagellin B, EGFRvIII peptide elevates CD8+ T cell numbers, lowers regulatory T cells (Tregs) in the brain, diminishes tumor volume, and extends survival in a GL261 glioblastoma mouse model.

NFAT inhibitor. Inhibits LPS or LPS plus IFN-γ-induced IL-12 p40, IL-12 p70, IL-23 and TNF secretion from bone marrow-derived macrophages (BMDMs). Also attenuates NO production and Nos2 mRNA expression in LPS-stimulated BMDMs. Improves symptoms in a mouse

Tkip is a specific inhibitor of JAK2. It binds to the autophosphorylation site of JAK2, thereby inhibiting JAK2 autophosphorylation and the phosphorylation of the IFN-γ receptor subunit IFNGR-1. Tkip can suppress the antiviral activity of IFN-γ and the expression of MHC class I molecules. Tkip is applicable in studies related to the IFN-γ signaling pathway.

PD-1/PD-L1 inhibitory peptide C8 disrupts the PD-1/PD-L1 interaction, leading to the activation of CD8+ and CD4+ T cells and an increase in IFN-γ secretion. In mouse models, PD-1/PD-L1 inhibitory peptide C8 has demonstrated antitumor activity.

PTD-N5-1 (N5-1) is an IRF5 inhibitory peptide. It can block the production of IL-12 induced by β-glucan in both wild-type and Clec2d-deficient bone marrow-derived dendritic cells (BMDC) that are activated by IFN-γ. PTD-N5-1 modulates antifungal immunity by inhibiting IRF5-mediated IL-12 production.

Eps8 peptide 327 is an HLA-A*2402-restricted peptide antigen derived from the Eps8 protein. It exhibits potent antitumor activity and significant cytotoxicity. Eps8 peptide 327 effectively inhibits cancer cell proliferation, induces apoptosis, and disrupts the EGFR signaling pathway by inhibiting the expression of downstream signals such as IL-2, TNF-α, and IFN-γ, as well as impeding the Eps8/EGFR interaction. It significantly suppresses tumor growth in HT-29 xenograft models.

TAT-327 is a cell-penetrating peptide known for selectively inserting into cancer cell membranes and exhibiting potent anti-tumor activity. It effectively inhibits cancer cell proliferation, induces apoptosis, and disrupts the EGFR signaling pathway by suppressing the expression of downstream signals (such as IL-2, TNF-α, and IFN-γ) and the interaction between Eps8 and EGFR. Additionally, TAT-327 significantly inhibits tumor growth in HT-29 xenograft models.