B7-33 – 6MG

B7-33 is a monochain peptide, a smaller analogue of the endogenous protein relaxin. Relaxin peptide is mostly constituted of 4 parts which consist a signal peptide, B chain, C chain and COOH terminal. More than 15 years ago when several groups tried to initially replicate these peptide structures by synthesizing them, others reported in studies that it is very insoluble and inactive. In the next few years investigators spent a lot of time trying to change the configuration and finally in 2016, after a series of subsequent serial research, scientists produced the first structural modification by preparation B chain together stretching COOH terminal, making an example soluble analog-the B7-33 peptide.

In addition to the structural difference, the peptide differs in a number of ways from the endogenous protein. Additionally, B7-33 peptide has been proposed to execute the effect through pERK pathway rather than cAMP pathway. The pERK pathway is a cellular signaling road that powers cell activity in manners that are often linked to cell thriving and apoptosis. In contrast, the cAMP pathway is related to a variety of cellular activities more closely related to energy balance and metabolism. H2-relaxin may have profibrotic effects on the cAMP pathway in which tumor genesis can be promoted. Otherwise, the peptide could bind with a high affinity for other RXFP-1 receptors. The peptide seems to be binding to these RXFP-1 receptors facilitating the pERK pathway which in turn allowed for a growth in the manufacturing of MMP-2 matrix metalloproteinase chemicals. MMP-2 is a proteolytic enzyme required for the degradation of extracellular matrix proteins and hence, involved in remodelling and repair processes. They also may act as tissue "scavengers" preventing fibrosis. Fibrosis can be defined as the development of increased amounts of fibrous connective tissue in a reparative or reactive process in any organ or tissue due to damage because fibrotic disorders are highly correlated with functional loss.

H2-relaxin, of which B7-33 is an analog, is a naturally expressed endogenous peptide, which was pharmacologically re-produced and designated B7-33. The relaxin protein class belongs to the H2-relaxin class of proteins and includes relaxin, H3-relaxin, insulin-like peptide-3 (INSL3), and insulin-like peptide-5 (INSL5). Each of these proteins has been theorized to have a broad spectrum of biological effects, including effects on gene function, as well as reproductive, musculoskeletal, and cardiovascular systems. Equivalent to H2-relaxin is the structurally different B7-33, a synthetic form that may possess anti-fibrotic properties.

The naturally occurring relaxins are thought to bind to four receptors, RXFP-1, RXFP-2, RXFP-3, and RXFP-4. Here is what each receptor does, in short:
- Some evidence was shown that the RXFP-1 receptor may play a role in sperm motility but a direct ligand for this receptor is still missing.
- Possibility of a role for RXFP-2 receptor in testicular development
- The primary results suggest that RXFP-3 receptor may be involved in circadian rhythm and sleep cycle regulation
- The RXFP-4 receptor has been implicated in the regulation of hunger hormone signaling pathways.

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