CJC-1295 without DAC

CJC-1295 without DAC in brief

CJC-1295 without DAC is a 29-residue analogue of the amino-terminal fragment of human growth hormone-releasing hormone, ending in an argininamide, with four changes to that sequence: D-alanine at 2, glutamine at 8, alanine at 15 and leucine at 27 (C152H252N44O42, 3367.9 g/mol). Three of those answer documented chemical liabilities of the parent fragment and the fourth raises receptor binding affinity. It carries none of the maleimide carrier-binding chemistry that the DAC suffix names, and is about 279 g/mol lighter than that molecule. Most of the evidence is analytical and enzymological; no receptor affinity or potency figure has been published for this exact molecule, and no structure exists.^[1,2,3,4,5]

CJC-1295 without DAC regulatory status

No FDA, EMA or Health Canada marketing authorisation for this peptide was found in Drugs@FDA, the European Medicines Agency medicines database or the Health Canada Drug Product Database (searched November 2026), and no registered trial of it was found: the one ClinicalTrials.gov record under the name CJC-1295, a terminated phase 2 study, was sponsored by ConjuChem, the developer of the maleimide conjugate. CJC-1295 is named on the World Anti-Doping Agency 2026 Prohibited List under S2.2.4 as a growth hormone-releasing hormone analogue, a non-specified substance prohibited at all times. The FDA's list of bulk drug substances that may present significant safety risks (current as of 22 April 2026) places a substance named CJC-1295, without specifying either form, among substances previously in category 2 whose nominations were withdrawn by the nominators, stating a possible risk of immunogenicity and complexities with peptide-related impurities and characterisation of the active ingredient, that the FDA has identified serious adverse events associated with CJC-1295 including increased heart rate and a systemic vasodilatory reaction, and that available clinical data are limited.^{[6,7,8,9,10,11,12]}

CJC-1295 without DAC at a glance

• A 29-residue peptide: positions 1 to 29 of human growth hormone-releasing hormone with four changes, D-alanine at 2, glutamine at 8, alanine at 15 and leucine at 27, ending in an argininamide. Formula C152H252N44O42, monoisotopic 3365.8936 Da.^[1,2]
• Each substitution answers a documented chemical liability of the parent fragment rather than a pharmacological aim: cleavage between residues 2 and 3 by dipeptidyl peptidase IV, rearrangement of asparagine 8 in water, oxidation of methionine 27. Alanine 15 is the exception, added because it raises receptor binding affinity.^[3,4,13]
• It is not the molecule sold with the DAC suffix, and only formula and mass separate the two. This one: C152H252N44O42, average about 3367.9 g/mol, monoisotopic 3365.9 Da, PubChem CID 56841945, CAS 863288-34-0, no maleimide and therefore no carrier chemistry. That one: C165H269N47O46, average about 3647.2 g/mol, monoisotopic 3645.0 Da, PubChem CID 91971820, CAS 446262-90-4, with an added lysine 30 whose side chain carries a maleimide that reacts with a free protein thiol, 279 g/mol heavier. Anti-doping laboratories write CJC-1295 for this peptide and name the other one CJC-1295 with drug affinity complex, while the PubChem record for this peptide carries synonyms belonging to the other.^{[1,2,14,15,16]}
• No three-dimensional structure exists, and no receptor-level measurement of this molecule has been published: no affinity at a cloned receptor, no functional potency, no comparison against the parent fragment.^[1,17,18,5]
• Status, in brief: no marketing authorisation in any register searched, and no registered trial of this peptide. CJC-1295 is named on the World Anti-Doping Agency 2026 Prohibited List under S2.2.4 as a growth hormone-releasing hormone analogue, prohibited at all times, and the FDA's list of bulk drug substances that may present significant safety risks records a withdrawn nomination for a substance named CJC-1295, stating that the agency has identified serious adverse events associated with it including increased heart rate and a systemic vasodilatory reaction. That listing does not say which of the two molecules it means. The regulatory status section above carries the agency's full wording.^{[6,7,8,9,11,12,10]}

What is CJC-1295 without DAC?

Human growth hormone-releasing hormone is a 44-residue hypothalamic peptide, recorded as residues 32 to 75 of a 108-residue precursor. Its first 29 residues with a C-terminal amide, the molecule called sermorelin, were long treated as the short form that keeps the parent's activity. That fragment has three chemical weaknesses, documented separately and unrelated to one another: plasma dipeptidyl peptidase IV removes the first two residues in a single cut, the asparagine at 8 rearranges in water through a cyclic aminosuccinimide, and the methionine at 27 oxidises to the sulfoxide.^[19,3,4]

A 1994 analogue series addressed those liabilities position by position, and added alanine at 15 because that change was already known to raise receptor binding affinity. Its most advanced candidate was [His1,Val2,Gln8,Ala15,Leu27]-hGRF(1-32)-OH. This molecule carries the same glutamine 8, alanine 15 and leucine 27 package, and reaches protease resistance differently, inverting the alanine at position 2 to its D-isomer rather than replacing the first two residues outright.^[4,20]

The qualifier in its name excludes a piece of chemistry rather than a substitution: the molecule sold with the DAC suffix adds a thirtieth residue whose side chain carries a maleimide, so it ends up covalently bound to a plasma protein and this one does not. The compact comparison of the two is in At a glance. A reader who arrived looking for modified GRF (1-29) is on the right page: that phrase is used for this compound widely, and this entry covers the tetrasubstituted 29-residue amide it denotes. The alias is nevertheless carried as proposed rather than verified, because no source printing a sequence could be found behind it: the only indexed paper using the exact phrase gives neither sequence nor mass, and a registry search returns nothing under it. The rest of the naming is better settled. A 2016 method defines CJC-1295 in exactly this molecule's terms, the earliest preparation identified under that name by a doping-control laboratory was a 29 amino acid amide, and every validated assay since treats it as its own analyte beside sermorelin and tesamorelin.^{[2,21,22,23,15,24]}

CJC-1295 without DAC structure and sequence

Read as a graph, the molecule is one unbranched chain of 29 amino acids, twenty-five of them reproducing the parent hormone's amino-terminal segment exactly and numbered the same way. Position 2 is the single departure from L-stereochemistry. The chain ends in a primary amide on arginine 29 rather than a free carboxylate, and nothing is attached to it: no lipid, polymer, sugar, metal or second chain. Containing neither cysteine nor methionine, it has no sulfur anywhere, which removes both the oxidation route that degrades the parent fragment and any possibility of thiol chemistry.^[1]

Written out against the parent, the difference is visible in one line. The hormone's first 29 residues read YADAIFTNSYRKVLGQLSARKLLQDIMSR; this molecule reads YaDAIFTQSYRKVLAQLSARKLLQDILSR, with the lower-case letter marking the D-residue. The changes are at position 2 (L-alanine to D-alanine), 8 (asparagine to glutamine), 15 (glycine to alanine) and 27 (methionine to leucine), and nowhere else; the parent sequence continues for a further fifteen residues where this chain stops at an argininamide.^[1,19,2]

The masses identify it in practice, and they sit close to its neighbours. At 3365.9 Da monoisotopic it is 10.1 Da above both sermorelin and CJC-1293, which share 3355.8 Da; in one validated plasma method all three elute within 0.2 minutes and the other two cannot be separated by retention time at all. A trifluoroacetate salt is catalogued one counterion heavier. The compound is measured as an intact peptide rather than as digest fragments, at or below 1 ng/mL in urine and below 50 pg/mL in plasma, and several of those methods recover it with antibodies raised against the parent hormone, so the four substitutions do not abolish recognition of the scaffold by a polyclonal reagent.^{[2,1,25,26,22,27,28,23,29,30]}

Nothing experimental fixes the shape. The closest measurement is proton NMR on a bovine 1-29 amide carrying leucine 27, and on its D-alanine 2 version, in 35 percent trifluoroethanol: both showed highly helical structure across residues 8 to 29 with only subtle differences at the amino termini, while their measured activities differed and an amino-terminally truncated version was about ten thousand times less potent. The authors concluded that solution secondary structure did not correlate with activity, so a helix measured in a helix-promoting cosolvent is not evidence about the active conformation. For this molecule there is no deposited structure and no conformer.^[31,1,17]

Two handling properties can be stated and one cannot. The chain carries five basic side chains (Arg11, Lys12, Arg20, Lys21, Arg29) and a free amino terminus against only two acidic ones (Asp3, Asp25), and because it ends in an amide there is no C-terminal carboxylate, so it is a basic peptide: computed from the sequence with standard residue dissociation constants the net charge at pH 7 is about +4 and the isoelectric point is near 11.0. That figure is a calculation stated as such, not a measurement, and it is given here because the competing figures in circulation sit on a page that also miscounts the residues. No measured appearance, aqueous solubility or melting figure exists on the PubChem record for this compound, whose experimental-properties section is empty, and none was copied from an uncited source.^[1]

One D-residue, the alanine at position 2; every other stereocentre is L, including the two isoleucines and the threonine, which each carry a second centre in the side chain. The chain is linear with no cyclisation and no bridging of any kind, and because it contains no cysteine it cannot form a disulfide with itself or with anything else. The PubChem IUPAC name records the position-2 residue as a (2R)-propanoyl unit, which is the D-configuration, and assigns (2S) to the remaining alpha carbons.^[1]

What studies on CJC-1295 without DAC show

Each card names the experimental system and what was measured. A result in one system is not evidence about another.

CJC-1295 without DAC compared with CJC-1295 with DAC and Sermorelin

Four things about the 3 compounds most often read beside it, on axes that can be checked: what kind of substance it is, its formula and mass, what public records settle about which substance it is, and the strongest three-dimensional evidence that exists for it. Every figure is the one stated on that compound's own page, which is where it is cited, so the two can never disagree. The table compares no effect, no potency and nothing a compound has been reported to do, and these compounds are not alternatives to one another.

Where the four substituted positions sit on the receptor contact map, and what the structures cannot say

The receptor this scaffold was built for is a class B1 G protein-coupled receptor with an extracellular domain and a seven-helix bundle. A cryo-EM structure of it bound to the parent hormone at 2.6 Angstrom shows the ligand as one continuous helix: amino terminus inserted into the helical core, the middle of the chain across the extracellular loops, residues past position 20 facing the extracellular domain. That is the only structural frame available, because nothing of this molecule has been determined. It also fits the finding that carboxy-terminally pegylated analogues of this scaffold kept high potency whatever the polymer mass, at the same end the DAC chemistry uses.^[32,33]

Read against that map, the four positions fall into three cases. Position 2 is the clearest: the structure assigns its side chain an ordinary hydrophobic contact, and inverting it did not change measured binding affinity in an adenopituitary membrane assay while abolishing the single peptidase cut. Position 15 is called substitution-tolerant there, and was among the most potent single substitutions in an independent alanine scan. Position 8 is more interesting, because asparagine 8 hydrogen bonds to the second extracellular loop and yet substitution there raised both potency and affinity, so the contact is not one another side chain cannot replace. Position 27 the structures cannot reach: it lies in the segment whose partners are the extracellular domain, which was not resolved in that map and was supplied by fitting a separately determined crystal structure.^[32,5,13,34]

The limits matter as much as the content. Every receptor-level number above was measured on the parent hormone or on a single substitution of the unmodified fragment, and these substitutions were chosen for chemical and enzymatic stability rather than receptor engagement, which is the distinction the binding assay was built to preserve. Four changes made together are not four made separately. The receptor is also not one protein: a splice variant differing only at its amino terminus couples selectively to beta-arrestins where the canonical form predominantly activates Gs.^[5,4,35]

What is still unknown about CJC-1295 without DAC

The name is the first problem and not a pedantic one. The compact comparison of the two molecules is in At a glance; what remains here is which records point which way. Several laboratories use CJC-1295 for this 29-residue peptide and name the conjugating molecule separately as CJC-1295 with drug affinity complex; one 2021 study lists them as two of its four analytes. Meanwhile the PubChem record for this compound carries CJC 1295 with DAC, DAC:GRF acetate and a maleimide-bearing systematic name among its synonyms, although its own formula contains neither the extra lysine nor the maleimide. A synonym, a registry number and a product label can each point to a different one of the two. A 2009 mouse study naming only CJC-1295 cannot be assigned to either, and neither can the FDA bulk-substance listing, which names CJC-1295 without saying which form it means.^{[2,14,1,36,12]}

One alias here is unverified, deliberately. Modified GRF (1-29) is attached to this molecule widely, but no source printing a sequence could be found behind it, and the only indexed paper using that exact phrase gives neither sequence nor mass. The equation is probably right and is not demonstrated, so it is carried as proposed and left out of this entry's name.^[24,15]

No potency figure of any kind exists for this molecule: no published affinity at a cloned receptor, no EC50 in a cAMP or reporter assay, no comparison against the parent hormone, sermorelin or the conjugating form. Every number on this page comes from a substitute, whether the 1-29 amide with one position changed, the sibling 1-32 series carrying three of the four substitutions, or the parent hormone in a receptor complex. That is a fair basis for why each substitution is present and a poor one for what the finished molecule does.^[5,13,4]

What is in a container sold under this name is a separate question. Preparations submitted under these names to a forensic laboratory were found to be glycine-extended analogues rather than the named compounds, a 2026 review states that composition in unregulated supply is itself uncertain, and the registry carries both acetate and trifluoroacetate forms. Two further gaps: the trypsin-like cleavage site at residues 12 to 13 in the 1-29 amide scaffold is untouched by all four substitutions and has never been examined in this molecule, and one 2022 assay paper classes the compound among ghrelin mimetics, which its sequence and lineage do not support.^[24,15,3,37]

Key papers on CJC-1295 without DAC

1. Qualitative identification of growth hormone-releasing hormones in human plasma by means of immunoaffinity purification and LC-HRMS/MS.

   Knoop A, Thomas A, Fichant E, Delahaut P, Schänzer W, Thevis M (2016), Analytical and Bioanalytical Chemistry · Immunoaffinity LC-HRMS/MS with in vitro and rodent stability

   The identity anchor, and the one paper to read first. It defines the compound by its four substitutions, prints its sequence and monoisotopic mass in a table beside sermorelin, CJC-1293 and tesamorelin, and shows that the D-alanine analogues produce no truncated metabolite where sermorelin does. Open access.

2. Enhanced stability and potency of novel growth hormone-releasing factor (GRF) analogues derived from rodent and human GRF sequences.

   Campbell RM, Stricker P, Miller R, Bongers J, Liu W, Lambros T, Ahmad M, Felix AM, Heimer EP (1994), Peptides · Analogue series with stability measurement and two bioassays

   The reason to believe glutamine 8, alanine 15 and leucine 27 are there for isomerisation, affinity and oxidation respectively, measured on a sibling analogue series rather than asserted. Read it knowing the constructs are 1-32 free acids with a different amino terminus.

3. Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma.

   Frohman LA, Downs TR, Heimer EP, Felix AM (1989), The Journal of Clinical Investigation · Plasma degradation enzymology

   The enzymology the D-alanine answers: one-step cleavage of the 2-3 bond by dipeptidyl peptidase IV, blocked by a D-residue at position 1 or 2. It also identifies the trypsin-sensitive site in the 1-29 amide that none of the substitutions addresses.

4. Identification of receptor-binding pharmacophores of growth-hormone-releasing factor in rat adenopituitary.

   Lefrançois L, Gaudreau P (1994), Neuroendocrinology · Radioligand binding scan on pituitary membranes

   The best evidence that the position-2 inversion is free at the receptor, from an assay built so that protease resistance could not be mistaken for affinity. Also the most complete map of which positions on this scaffold cannot be touched.

5. Human growth hormone-releasing hormone hGHRH(1-29)-NH2: systematic structure-activity relationship studies.

   Cervini LA, Donaldson CJ, Koerber SC, Vale WW, Rivier JE (1998), Journal of Medicinal Chemistry · Systematic structure-activity relationship study

   An independent scan that agrees with the design rationale on positions 8 and 15 and supplies the one direct caution about substituting position 27 at all.

6. Structural basis for activation of the growth hormone-releasing hormone receptor.

   Zhou F, Zhang H, Cong Z, Zhao LH, Zhou Q, Mao C, Cheng X, Shen DD, Cai X, Ma C, Wang Y, Dai A, Zhou Y, Sun W, Zhao F, Zhao S, Jiang H, Jiang Y, Yang D, Xu HE, Zhang Y, Wang MW (2020), Nature Communications · Cryo-EM structure with alanine scanning and molecular dynamics

   The near-atomic structure of the receptor with a peptide in it, and the source for where positions 8 and 15 sit in the contact map. Open access. Read it knowing the ligand is the 44-residue hormone, that the extracellular domain was fitted rather than resolved, and that position 27 therefore has no observed contact.

7. Glycine-modified growth hormone secretagogues identified in seized doping material.

   Gajda PM, Holm NB, Hoej LJ, Rasmussen BS, Dalsgaard PW, Reitzel LA, Linnet K (2019), Drug Testing and Analysis · Identification by LC-HRMS against reference standards

   Short, and the most useful corrective on this page: four preparations named after four compounds in this field, examined by a forensic laboratory, none of which contained the compound it named.

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