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BRINP2-related peptide

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Other namesBRINP2-related peptide; BRP
Routes of
administration
Subcutaneous, Intravenous, Intraperitoneal
Drug classPeptide-based metabolic modulator
Legal status
  • Investigational
BRINP2-related peptide
Structural formula of BRP peptide
Clinical data
Other namesBRINP2-related peptide; BRP
Routes of
administration
Subcutaneous, Intravenous, Intraperitoneal
Drug classPeptide-based metabolic modulator
Legal status
Legal status
  • Investigational
Pharmacokinetic data
MetabolismProteolytic degradation (Arg-Arg cleavage site)[1]
Chemical and physical data
FormulaC68H117N25O14S
Molar mass1540.91 g·mol−1
3D model (JSmol)
  • CC[C@H](C)[C@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@@H](N)[C@@H](C)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CS)C(N)=O
  • InChI=1S/C68H117N25O14S/c1-10-37(8)53(93-57(99)43(21-16-24-81-68(76)77)85-62(104)48(29-40-31-78-33-82-40)90-64(106)52(70)38(9)94)65(107)91-46(27-36(6)7)58(100)84-41(19-14-22-79-66(72)73)55(97)83-42(20-15-23-80-67(74)75)56(98)86-44(25-34(2)3)59(101)88-47(28-39-17-12-11-13-18-39)61(103)89-49(30-51(69)95)63(105)87-45(26-35(4)5)60(102)92-50(32-108)54(71)96/h11-13,17-18,31,33-38,41-50,52-53,94,108H,10,14-16,19-30,32,70H2,1-9H3,(H2,69,95)(H2,71,96)(H,78,82)(H,83,97)(H,84,100)(H,85,104)(H,86,98)(H,87,105)(H,88,101)(H,89,103)(H,90,106)(H,91,107)(H,92,102)(H,93,99)(H4,72,73,79)(H4,74,75,80)(H4,76,77,81)/t37-,38+,41-,42-,43-,44-,45-,46-,47-,48-,49-,50-,52-,53-/m0/s1
  • Key:HMJIRJDBVYKLDC-KVBBLKIJSA-N

BRINP2-related peptide (BRP) is a synthetic peptide that displays anti-obesity action similar to semaglutide. It does this without significant muscle loss or anxiety and without impacting bowel movement when administered to mice and pigs.[2] BRP primarily stimulates receptors in the hypothalamus and is consistent with GPCR activation leading to stimulation of CREB and Fos activity in neuronal cells.[1]

Researchers at Stanford University derived BRP from the BRINP2 protein, corresponding to amino acids 386–397 (THRILRRLFNLC) of BRINP2.[1][3] This 12-amino acid peptide is flanked by KK and KR recognition sites within the BRINP2 protein, which are cleaved by proprotein convertases to release the peptide. BRP has been detected in human cerebrospinal fluid by mass spectrometry.[1] Additionally, BRP undergoes C-terminal amidation, resulting in the sequence THRILRRLFNLC-NH2. The non-amidated form of the peptide is inactive.[1]

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