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MBP (84-97) – VVHFFKNIVTPRTP

 

Myelin Basic Protein

MBP (Myelin Basic Protein – UniProtKB – P04370) is a major constituent of the myelin in nerves. This protein permits the maintain of the myelin structure. MBP contains various epitopes implicated in Multiple Sclerosis.

MBP (84-97) induces EAE

The MBP 84-97 peptide is an immunodominant epitope of MBP. The sequence is conserved in various species (guinea pig, human…). MBP84-97 is used to induce EAE (Experimental Autoimmune Encephalomyelitis).

MBP 84-97 - VVHFFKNIVTPRTP

MBP84-97 specifications

PADRE peptide MHC HLA Sequence : VVHFFKNIVTPRTP – Purity : > 95%
PADRE peptide adjuvant MW : 1654.95 g / mol (C79H123N21O18)
PADRE peptide price For research use
PADRE peptide Counter-Ion : TFA Salts (see option TFA removal)
Peptide library synthesis Delivery format : Freeze dried in polypropylene 2mL microtubes
buy synthesized peptides Other names : Myelin Basic Protein (84-97)
peptide solubility guidelines Peptide Solubility Guideline
buy peptide price Bulk peptide quantities available

 

MBP 84-97 related product

 

Prices

Product catalog Size Price € HT Price $ USD
SB0181-1MG 1 mg 100 125
SB0181-5MG 5 mg 350 440

References

Bioorg Med Chem . 2017 Jan 15;25(2):528-538. doi: 10.1016/j.bmc.2016.11.029. Epub 2016 Nov 19

Cyclic citrullinated MBP87–99 peptide stimulates T cell responses: Implications in triggering disease

 Amino acid mutations to agonist peptide epitopes of myelin proteins have been used to modulate immune responses and experimental autoimmune encephalomyelitis (EAE, animal model of multiple sclerosis). Such amino acid alteration are termed, altered peptide ligands (APL). We have shown that the agonist myelin basic protein (MBP) 87–99 epitope (MBP87–99) with crucial T cell receptor (TCR) substitutions at positions 91 and 96 (K91,P96 (TCR contact residues) to R91,A96; [R91,A96]MBP87–99) results in altered T cell responses and inhibits EAE symptoms. In this study, the role of citrullination of arginines in [R91,A96]MBP87–99 peptide analog was determined using in vivo experiments in combination with computational studies. The immunogenicity of linear [Cit91,A96,Cit97]MBP87–99 and its cyclic analog – cyclo(87–99)[Cit91,A96,Cit97]MBP87–99 when conjugated to the carrier mannan (polysaccharide) were studied in SJL/J mice. It was found that mannosylated cyclo(87–99)[Cit91,A96,Cit97]MBP87–99 peptide induced strong T cell proliferative responses and IFN-gamma cytokine secretion compared with the linear one. Moreover, the interaction of linear and cyclic peptide analogs with the major histocompatibility complex (MHC II, H2-IAs) and TCR was analyzed using molecular dynamics simulations at the receptor level, in order to gain a better understanding of the molecular recognition mechanisms that underly the different immunological profiles of citrullinated peptides compared to its agonist native counterpart MBP87–99 epitope. The results demonstrate that the citrullination of arginine in combination with the backbone conformation of mutated linear and cyclic analogs are significant elements for the immune response triggering the induction of pro-inflammatory cytokines

J Autoimmun . 2017 Nov;84:1-11. doi: 10.1016/j.jaut.2017.06.005. Epub 2017 Jun 20

Targeting the GM-CSF receptor for the treatment of the CNS autoimmunity

In multiple sclerosis (MS), there is a growing interest in inhibiting the pro-inflammatory effects of granulocyte-macrophage colony-stimulating factor (GM-CSF). We sought to evaluate the therapeutic potential and underlying mechanisms of GM-CSF receptor alpha (Rα) blockade in animal models of MS. We show that GM-CSF signaling inhibition at peak of chronic experimental autoimmune encephalomyelitis (EAE) results in amelioration of disease progression. Similarly, GM-CSF Rα blockade in relapsing-remitting (RR)-EAE model prevented disease relapses and inhibited T cell responses specific for both the inducing and spread myelin peptides, while reducing activation of mDCs and inflammatory monocytes. In situ immunostaining of lesions from human secondary progressive MS (SPMS), but not primary progressive MS patients shows extensive recruitment of GM-CSF Rα+ myeloid cells. Collectively, this study reveals a pivotal role of GM-CSF in disease relapses and the benefit of GM-CSF Rα blockade as a potential novel therapeutic approach for treatment of RRMS and SPMS.