BRP/BRINP2-related peptide

BRP/BRINP2-related peptide

• Handling and Storage of Synthetic Peptides
• Material Safety Data Sheets (MSDS)

Batch to batch variation of the purity

H-THRILRRLFNLC-OH

H-Thr-His-Arg-Ile-Leu-Arg-Arg-Leu-Phe-Asn-Leu-Cys-OH

12

95.33%

C₆₈H₁₁₆N₂₄O₁₅S

1541.86

Synthetic

Powder

THRILRRLFNLC is a 12-mer peptide, also known as BRINP2-related peptide (BRP), which was discovered through Peptide Predictor, a computational-functional approach based on prohormone convertase (PCSK) prohormone processing. It is generated by the cleavage of the 78-kDa secreted parent protein BRINP2 by enzymes such as PCSK1. The KK and KR cleavage sites on both sides of it can be recognized by proconvertases, releasing this peptide. Structural prediction indicates that it may exist in an α-helical or linear conformation. BRINP2 is mainly expressed in the brains of mice, humans, and pigs. BRP has been detected in both human cerebrospinal fluid and mouse brains. Its concentration in human cerebrospinal fluid ranges from 700 pM to 3 nM, and it also has a certain concentration in mouse brains. BRP can effectively reduce food intake in mice and pigs and has anti-obesity effects. In mice, it can significantly reduce food intake, and this effect can be observed in both male and female mice, as well as in different obesity states (such as lean mice and diet-induced obese mice). In pigs, it can also reduce food intake. Its mechanism of action is independent of known appetite-regulating pathways such as GLP1R, leptin, and MC4R. Instead, it activates the central CREB-FOS signaling pathway, specifically by activating some regions of the hypothalamus (such as the dorsomedial hypothalamic nucleus, preoptic hypothalamic nucleus, tuberal nucleus, and arcuate nucleus, etc.). BRP does not cause changes in pancreatic activity, that is, it does not affect blood glucose levels and insulin secretion. It also does not induce nausea or aversion, showing certain advantages in improving metabolism.

Normally, this peptide will be delivered in lyophilized form and should be stored in a freezer at or below -20 °C. For more details, please refer to the manual: Handling and Storage of Synthetic Peptides

• Coassolo L, B Danneskiold-Samsøe N, Nguyen Q, Wiggenhorn A, Zhao M, Wang DC, Toomer D, Lone J, Wei Y, Patel A, Liparulo I, Kavi D, Wat LW, Reghupaty SC, Kim JJ, Asemi T, Bielczyk-Maczynska E, Li VL, Moya-Garzon MD, Krentz NAJ, Stahl A, Chou DH, Luo L, Svensson KJ. Prohormone cleavage prediction uncovers a non-incretin anti-obesity peptide. Nature. 2025 Mar 5. doi: 10.1038/s41586-025-08683-y. Epub ahead of print. PMID: 40044869.

Trifluoroacetic acid (TFA) has a significant impact on peptides due to its role in the peptide synthesis process.

TFA is essential for the protonation of peptides that lack basic amino acids such as Arginine (Arg), Histidine (His), and Lysine (Lys), or ones that have blocked N-termini. As a result, peptides often contain TFA salts in the final product.

TFA residues, when present in custom peptides, can cause unpredictable fluctuations in experimental data. At a nanomolar (nM) level, TFA can influence cell experiments, hindering cell growth at low concentrations (as low as 10 nM) and promoting it at higher doses (0.5–7.0 mM). It can also serve as an allosteric regulator on the GlyR of glycine receptors, thereby increasing receptor activity at lower glycine concentrations.

In an in vivo setting, TFA can trifluoroacetylate amino groups in proteins and phospholipids, inducing potentially unwanted antibody responses. Moreover, TFA can impact structure studies as it affects spectrum absorption.