CJC-1295 raises a handful of sensible questions. This page answers them in order, starting with the fundamentals and moving to applications.
Reviewed 2026-04-08. Anything still debated is marked as such rather than presented as settled.
The peptide binds GHRH receptors on somatotroph cells within the anterior pituitary, triggering a signalling cascade that increases growth hormone secretion. Its improved resistance to dipeptidyl peptidase IV degradation distinguishes it from the parent hormone. In the DAC-bearing version, a maleimide group reacts with a cysteine residue on serum albumin, forming a covalent bond that keeps the peptide in circulation far longer. That albumin attachment is the central design feature separating the two research variants.
Pharmacokinetic behaviour differs sharply between the two forms. The DAC-bearing peptide shows an extended circulation time measured in days, whereas the version without the complex is cleared within roughly half an hour. This gap shapes how researchers design dosing schedules in animal models. Whether the prolonged presence of the DAC form produces effects meaningfully different from the short-acting variant remains an open question, since comparative human data are scarce.
CJC-1295 belongs to a family of synthetic peptides modeled on growth hormone-releasing hormone, the hypothalamic signal that prompts the pituitary to release growth hormone. The compound is built from the first twenty-nine amino acids of the natural human sequence, a fragment that retains full receptor binding capacity. Native growth hormone-releasing hormone is degraded quickly in circulation, so the fragment alone has limited practical value. Early work therefore focused on chemical modifications that preserve receptor binding while slowing enzymatic breakdown. The result is a molecule described in the literature as a long-acting analog of the natural hormone.
| Property | Value | Notes |
|---|---|---|
| Molecular weight (with DAC) | ~3647 Da | Calculated from the full amino acid sequence |
| Molecular weight (without DAC) | ~3368 Da | Mod GRF(1-29) variant |
| Appearance | White lyophilized powder | Typical form supplied for research |
| Solubility | Soluble in water | Dissolves in aqueous buffers |
| Receptor target | GHRH receptor | Expressed on pituitary somatotroph cells |
Laboratory handling centers on minimizing exposure to water, heat and oxygen before use. Working solutions are typically prepared in sterile water or a mild buffer, and any residual particulate matter is removed by filtration. When the powder dissolves slowly, a small proportion of acetonitrile or dilute acetic acid is sometimes added as a co-solvent. Containers are kept sealed and desiccated between uses. Records of lot number, reconstitution date and storage conditions support later comparison of results across experiments.
Identity and purity are established with reversed phase high performance liquid chromatography coupled to mass spectrometry. The chromatographic step separates the target peptide from truncated sequences and deletion products, while the mass measurement confirms the expected molecular weight to within a fraction of a dalton. Because the two common variants differ by the presence of the linker, mass alone can distinguish them in the unconjugated state. Amino acid analysis and peptide mapping are used when sequence level confirmation is required.
The peptide backbone includes a D-alanine at position two, which resists cleavage by dipeptidyl peptidase IV, and several other substitutions that reduce degradation. Its molecular weight is roughly 3.4 kDa without the linker and about 3.6 kDa with it. The molecule is water soluble and is normally supplied as a lyophilized powder. Precise sequence and mass values depend on which variant is described, so technical documents usually state the exact form being referenced.
CJC-1295 is a synthetic peptide designed as a long-acting analogue of growth hormone-releasing hormone (GHRH). Its structure derives from the first 29 amino acids of native GHRH, a fragment often called GRF(1-29). Four substitutions were introduced to slow enzymatic breakdown and extend activity relative to the natural sequence. The compound was developed by ConjuChem as part of a broader effort to improve the pharmacokinetic profile of peptide hormones. It is studied in laboratory and clinical research settings rather than appearing as a naturally occurring substance.
Two related forms circulate in technical discussion under the same family name. The original version carries a drug affinity complex (DAC) that binds covalently to serum albumin after administration, and this linkage substantially extends circulation time. A second form, frequently written as modified GRF(1-29) or CJC-1295 without DAC, lacks that linker and clears much faster. The naming is a frequent source of confusion because the shorthand CJC-1295 can refer to either form depending on the source. Reports sometimes fail to specify which variant was studied.
Two forms circulate in research settings and are frequently confused. One carries the drug affinity complex and is often written as CJC-1295 with DAC; the other lacks that group and is usually called modified GRF(1-29). The two share the same core sequence but differ sharply in how long they persist in blood. Products labelled only as CJC-1295 normally refer to the version carrying the complex. Documentation that omits the distinction leaves the intended molecule ambiguous.
CJC-1295 is a synthetic peptide built as a long-acting analogue of growth hormone-releasing hormone. Its backbone matches the first twenty-nine residues of the natural human hormone, with four amino acid substitutions added to slow enzymatic breakdown. A reactive maleimide group, commonly termed the drug affinity complex, allows the peptide to attach to circulating albumin after administration. That albumin attachment keeps the molecule in the bloodstream for an extended period instead of being cleared within minutes.
The compound emerged from work at a Canadian biotechnology firm in the early 2000s. Early human studies examined its effect on growth hormone and insulin-like growth factor 1 in healthy volunteers and in people with HIV-associated fat redistribution. Reports described sustained increases in both markers after a single injection. Development did not advance to regulatory approval, and the clinical programme was later discontinued. The molecule is now encountered mainly as a research chemical rather than a marketed medicine.
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In spectroscopy, absorbance (abbreviated as A) is a logarithmic value which describes the portion of a beam of light which does not pass through a sample. Whilst the name refers to the absorption of light, other interactions of light with a sample (reflection, scattering) may also contribute to attenuation of the beam passing through the sample. The term "internal absorbance" is sometimes used to describe beam attenuation caused by absorption, while "attenuance" or "experimental absorbance" can be used to emphasize that beam attenuation can be caused by other phenomena.
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The later demise of the National Assembly proved to be a major setback for Political Catholicism. In the Kingdom of Prussia, the revised constitution of 1850 granted liberties, which in parts even exceeded those of the Frankfurt draft constitution, yet two years later the minister for culture, von Raumer, issued decrees directed mainly against the Jesuits. In reaction this led to a doubling of Catholic representatives in the subsequent elections and the formation of a Catholic club in the Landtag of Prussia. In 1858, when the "New Era" governments of Wilhelm I adopted more lenient policies, the club renamed itself "Fraction of the Centre" in order to open itself up to include non-Catholics. This name stemmed from the fact that in the Landtag the Catholic representatives were seated in the centre, between the Conservatives on the right and the Liberals on the left. Faced with military and constitutional issues, where there was no definite Church position, the group soon disintegrated and disappeared from parliament after 1867.
=== Redox === p-Hydroxybenzoate hydroxylase (PHBH) catalyzes the oxygenation of p-hydroxybenzoate (pOHB) to 3,4-dihyroxybenzoate (3,4-diOHB); FAD, NADPH and molecular oxygen are all required for this reaction. NADPH first transfers a hydride equivalent to FAD, creating FADH−, and then NADP+ dissociates from the enzyme. Reduced PHBH then reacts with molecular oxygen to form the flavin-C(4a)-hydroperoxide. The flavin hydroperoxide quickly hydroxylates pOHB, and then eliminates water to regenerate oxidized flavin. An alternative flavin-mediated oxygenation mechanism involves the use of a flavin-N(5)-oxide rather than a flavin-C(4a)-(hydro)peroxide.
Sources: en.wikipedia.org
There was low- to moderate-strength evidence of no benefit for most of the other medications used in RCTs, which included antidepressants (bupropion, mirtazapine, sertraline), antipsychotics (aripiprazole), anticonvulsants (topiramate, baclofen, gabapentin), naltrexone, varenicline, citicoline, ondansetron, prometa, riluzole, atomoxetine, dextroamphetamine, and modafinil.
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Sources: en.wikipedia.org
The synthetic peptide keeps the receptor-binding region of GHRH but carries substitutions that resist enzymatic cleavage. In the DAC version, an added group also anchors the molecule to albumin, extending its presence in the bloodstream.
The maleimide group forms a covalent link with albumin, an abundant blood protein. This attachment slows clearance, so a single administration persists much longer than the unmodified peptide. The feature is the main reason the two variants are handled differently in study design.
It is not an approved therapeutic product in major regulatory jurisdictions. It appears in research chemical catalogs and scientific literature rather than pharmacy shelves. Clinical development was limited and did not reach approval.
The mass difference from the linker is large enough for routine detection by mass spectrometry. The unconjugated form gives a single sharp signal at its expected weight. Material that has already reacted with albumin shows a much higher mass and a broadened chromatographic peak.