@LINE Here is another from amazon similar to waynes post. This methylene blue is United States Pharmacopeia (USP) grade also, which is generally accepted for food, drug, and medicinal use and has heavy metal analysis.
https://www.amazon.com/Methylene-Blue-Pharmaceutical-Grade-Solution/dp/B0BC2GGYYS/r at 1%
The first question is whether its mainly the anti inflammatory (NLRP3 inhibition for example) in the earlier stages during higher inflammation that is what people are after, as palmitoylethanolamide (PEA) which uses one pathway (PPAR-a) and has known effects to help restore the gut barrier and microbiome/short chain fatty acid profile and dozens of others that work in various ways I can post a list could be alternatives.
PPAR-a also inhibits STING. timing is important where inflammation is actually very important in early stages of viral infection (Type I interferon mediates an important innate immune response against viral infection by directly inhibiting viral replication.) and if you inhibit it too early there can be higher viral titers when challenged with influenza A virus etc during the early stages of infection, but it IS beneficial to inhibit in a later stage if the virus was able to replicate and was at that later stage causing inflammation because you did not have a good immune response early on, as inhibiting in later stages experienced less tissue damage to lungs. .
Butyrate I've also mentioned is a lipid produced by intestinal bacteria that can regulate inflammation throughout the body. Here we show for the first time that butyrate influences the innate antiviral immune response mediated by type I IFNs. A majority of antiviral genes induced by type I IFNs were repressed in the presence of butyrate, resulting in increased virus infection and replication in cells. We found that butyrate increases cellular infection and virus replication in influenza virus, reovirus, and human immunodeficiency virus infections. In sum, the net effect of butyrate on infection with three divergent RNA viruses was an increase in cellular infection and replication. Further exploring this phenomenon, we found that addition of butyrate to cells deficient in type I interferon (IFN) signaling did not increase susceptibility to virus infection. Accordingly, we discovered that butyrate suppressed levels of specific IFN stimulated gene (ISG) products in human and mouse cells. Butyrate did not inhibit IFN-induced phosphorylation of transcription factors STAT1 and STAT2 or their translocation to the nucleus, indicating that IFN signaling was not disrupted. Rather, our data are suggestive of a role for inhibition of histone deacetylase activity by butyrate in limiting ISG induction including RIG-I. Global transcript analysis revealed that butyrate increases expression of more than 800 cellular genes, but represses IFN-induced expression of 60% of ISGs
https://www.biorxiv.org/content/10.1101/2020.02.04.934919v1
Metabolic Control of Viral Infection through PPAR-α Regulation of STING Signaling. PPAR ligands (activators) are immunosuppressive and can increase susceptibility to infection therefore it appears should not be increased greatly in early infection. PPARs mechanisms of action are diverse and include repression of NFκB and AP-1 DNA binding, regulation of nitric oxide, inhibition of dendritic cell maturation, reduction of cytokine expression by effector T cells, and inhibition of leukocyte recruitment to sites of inflammation. Activation of PPAR-α with specific agonists increased herpesvirus replication and reactive oxygen species (ROS) production. ROS inhibited activation of stimulator of interferon (STING), an ER adapter that induces type I interferon downstream of cytoplasmic DNA recognition. Although high ROS induces inflammasome activation and cytokine production, we found that ROS inhibited interferon production. Treatment of mice with a clinically relevant agonist of PPAR-α increased herpesvirus replication and pathogenesis, comparable to levels observed previously in type I interferon receptor knockout mice. These findings show that activated PPAR-α regulates immunity to cytoplasmic DNA, inhibits interferon production, and increases susceptibility to viral infection (in early stages of infection). Moreover, these results demonstrate that ROS inhibit STING activation and induction of interferon
https://www.biorxiv.org/content/10.1101/731208v3
STING (stimulator of interferon genes) protein regulates metabolic homeostasis through inhibition of the fatty acid desaturase 2 (FADS2) rate-limiting enzyme in polyunsaturated fatty acid (PUFA) desaturation.
STING agonists directly activated FADS2-dependent desaturation, promoting metabolic alterations. PUFAs in turn inhibited STING, thereby regulating antiviral responses and contributing to resolving STING-associated inflammation. Thus, we have unveiled a negative regulatory feedback loop between STING and FADS2 that fine-tunes inflammatory responses.
https://pubmed.ncbi.nlm.nih.gov/34986331/
