CJC-1295 (without DAC) vs GHRP-2

CJC-1295 (without DAC)

CJC-1295 without DAC, also called modified GRF (1-29), is a 29-residue synthetic analogue of growth hormone-releasing hormone (GHRH). Native GHRH has 44 residues, but its first 29 carry the receptor-binding activity, and this peptide is built on that shortened sequence with four amino-acid substitutions intended to slow breakdown. The name causes confusion: CJC-1295 originally referred to a version carrying a drug affinity complex (DAC), a reactive linker that binds albumin and greatly prolongs circulation. The form described here lacks that linker. Human studies of the DAC version exist but are few; published work on the form without DAC is thinner still, and much of what is said about it is inferred from the parent hormone.

GHRP-2

GHRP-2, also known by the non-proprietary name pralmorelin, is a synthetic hexapeptide that activates the ghrelin receptor, GHS-R1a. Three of its six residues are D-amino acids, including the non-natural D-2-naphthylalanine, a design feature shared with other synthetic growth hormone-releasing peptides. These compounds were developed by screening for growth hormone release before their receptor had been identified; ghrelin, the receptor's natural ligand, was discovered afterwards. GHRP-2 has been examined in receptor and pituitary cell assays, in animal studies, and in short human endocrine studies that measured hormone secretion. Longer-term human data are sparse, and it is not selective for growth hormone, since rises in other pituitary and adrenal hormones have also been recorded.

How CJC-1295 (without DAC) acts

Like native GHRH, the peptide has been reported to bind the GHRH receptor, a class B G protein-coupled receptor on somatotroph cells of the anterior pituitary. Receptor activation couples to Gs, raising intracellular cAMP and releasing stored growth hormone; circulating growth hormone in turn drives IGF-1 production, mainly in the liver. The substitutions, D-alanine at position 2, glutamine at 8, alanine at 15 and leucine at 27, were chosen to resist cleavage by dipeptidyl peptidase-4 and to reduce deamidation and oxidation at vulnerable residues. Without the albumin-binding linker its half-life is short, and pharmacokinetic data specific to this form are sparse.

How GHRP-2 acts

GHRP-2 has been reported to act as an agonist at GHS-R1a, a G protein-coupled receptor present on somatotroph cells of the anterior pituitary and on neurons in the hypothalamus. In somatotrophs the receptor couples mainly to Gq and phospholipase C, and the rise in intracellular calcium that follows triggers growth hormone secretion. This route is separate from that of growth hormone-releasing hormone (GHRH), which acts through its own receptor and cyclic AMP. Part of the response is thought to be hypothalamic, through effects on GHRH neurons and on somatostatin signalling. In human studies, modest increases in ACTH, cortisol and prolactin have been reported alongside growth hormone.

The records side by side

• Type: CJC-1295 (without DAC), GHRH analog (Modified GRF 1-29); GHRP-2, Growth hormone secretagogue (GHRP)
• Length: CJC-1295 (without DAC), not recorded; GHRP-2, 6 amino acids
• Molecular weight: CJC-1295 (without DAC), 3647.2 g/mol; GHRP-2, 818.0 g/mol
• Molecular formula: CJC-1295 (without DAC), C165H269N47O46; GHRP-2, C45H55N9O6

Reading a comparison

A comparison places two records side by side; it does not merge them. Each description above is drawn from that compound's own record, and the two were not necessarily characterised by the same methods, at the same time, or to the same level of detail. Before comparing any attribute, it is worth establishing that both records describe the substance you think they describe — names are not identifiers, and two entries sharing a name can differ in salt form, stereochemistry or the convention used to state a mass. Where a figure carries no method beside it, the comparison is between two reported numbers rather than between two measurements.