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Cjc-1295 Structure And Mechanism — Background and Details

By Editorial Desk · published 2026-04-19 · last reviewed 2026-05-10 · Faq

A practical reference on reversed-phase HPLC: what it is, how it behaves, what the literature reports, and where the honest uncertainties sit.

This page was last updated on 2026-05-10 and is reviewed periodically as new material appears.

CJC-1295 Structure And Mechanism

CJC-1295 is a synthetic analogue of growth hormone-releasing hormone, built on the 29-amino-acid GHRH(1-29) fragment. Four substitutions distinguish it from the natural sequence: D-alanine at position 2, glutamine at position 8, alanine at position 15, and leucine at position 27. These changes reduce enzymatic cleavage and extend the peptide's persistence in circulation. The compound is discussed in two forms, one carrying a drug affinity complex and one without it.

The drug affinity complex is a maleimidopropionic acid group attached to a lysine side chain. It reacts with the free thiol of cysteine-34 on circulating albumin, forming a covalent bond. This conjugation keeps the peptide in the bloodstream and shields it from rapid renal filtration and proteolysis. Reported circulation half-lives for the albumin-bound form fall in the range of roughly six to nine days in early human studies.

Binding to GHRH receptors on pituitary somatotroph cells triggers cyclic AMP signaling and stimulates growth hormone synthesis and release. Because the peptide acts upstream of the pituitary, effects are mediated through endogenous growth hormone rather than direct receptor activation in peripheral tissues. Increases in insulin-like growth factor 1 are generally described as a downstream consequence. Most published human exposure data come from small early-stage studies, and the clinical significance of the pharmacokinetic profile remains incompletely characterized.

Compound Identity and Development History

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.

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.

Cjc-1295 at a glance

PropertyValueNotes
Physical formLyophilized white powderSupplied as a freeze-dried solid for research use
Molecular weightApproximately 3,647 Da (DAC form)Lower for the variant lacking the albumin-binding moiety
SolubilitySoluble in water and aqueous bufferTypically dissolved in sterile or bacteriostatic water
Typical storage temperature−20 °C or belowDry powder, desiccated and protected from light
Common analytical methodReversed-phase HPLC with mass spectrometryUsed for purity estimation and identity confirmation

Background and Molecular Design

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.

Two forms circulate under the CJC-1295 name, and they differ by a single appended group. The version without a drug affinity complex carries four substitutions along the peptide chain, including a D-alanine near the amino terminus and replacements at three other positions. These changes block the enzyme dipeptidyl peptidase IV and remove a methionine residue that is prone to oxidation. The modified fragment is frequently labeled MOD GRF 1-29. Naming conventions are inconsistent across informal sources, which is a common source of confusion.

The second form adds a maleimide-bearing linker to the lysine at the carboxyl end. This group reacts with cysteine-34 on circulating serum albumin, forming a covalent bond that keeps the peptide in the bloodstream for far longer. ConjuChem developed the molecule as a way to extend the action of a peptide without frequent administration. The albumin attachment is the defining structural feature of the drug affinity complex version. Whether continuous exposure produces effects distinct from shorter pulses remains an unresolved research question.

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Analytical Characterization and Storage

Stability depends heavily on physical state. A lyophilized powder kept dry, desiccated, and shielded from light typically holds its integrity for months to years at minus twenty degrees Celsius, and longer at minus eighty. Once dissolved, the peptide becomes far more vulnerable, since peptide bond hydrolysis, oxidation of susceptible residues, and aggregation all proceed faster in solution. Buffers near neutral pH are generally gentler than strongly acidic or alkaline conditions. Repeated freeze-thaw cycles and exposure to air-liquid interfaces during vigorous mixing cause losses that are easy to overlook.

Verification matters because research peptides vary widely in quality. A certificate of analysis is only as reliable as the method behind it, and a single chromatographic trace reveals little about counter-ions, residual solvents, or water content. Independent laboratories commonly pair mass confirmation with chromatographic purity and, where relevant, quantify water along with acetate or trifluoroacetate content. Reported purity figures are not standardized across suppliers, so a stated value such as ninety-eight percent is not directly comparable unless the analytical method, column, and detection wavelength accompany it.

Supporting material

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==== High-throughput solvothermal synthesis ==== In high-throughput solvothermal synthesis, a solvothermal reactor with multiple cavities is used. Such a reactor is sometimes referred to as a multiclav. The reactor block or reactor insert is made of stainless steel and may contain, for example, 24 reaction chambers arranged in four rows. These miniaturized teflon reactors can hold up to 2 mL. The reactor block is sealed in a stainless steel autoclave with the filled reactors inserted into the bottom of the reactor, the teflon reactors are sealed with two teflon films, and the reactor top side is put on. The autoclave is then closed in a hydraulic press. The sealed solvothermal reactor is then be subjected to a temperature-time program. The reusable teflon film serves to withstand the mechanical stress, while the disposable teflon film seals the reaction vessels. After the reaction, the products can be isolated and washed in parallel in a vacuum filter device. On the filter paper, the products are then present separately in a so-called sample library and can subsequently be characterized by automated X-ray powder diffraction. The informations obtained are then used to plan further syntheses.

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Sources: en.wikipedia.org

Notes from published material

The use of pulses of different durations, frequencies, or shapes in specifically designed patterns or pulse sequences allows production of a spectrum that contains many different types of information about the molecules in the sample. In multi-dimensional nuclear magnetic resonance spectroscopy, there are at least two pulses: one leads to the directly detected signal and the others affect the starting magnetization and spin state prior to it. The full analysis involves repeating the sequence with the pulse timings systematically varied in order to probe the oscillations of the spin system are point by point in the time domain. Multidimensional Fourier transformation of the multidimensional time signal yields the multidimensional spectrum. In two-dimensional nuclear magnetic resonance spectroscopy (2D-NMR), there will be one systematically varied time period in the sequence of pulses, which will modulate the intensity or phase of the detected signals. In 3D-NMR, two time periods will be varied independently, and in 4D-NMR, three will be varied. There are many such experiments. In some, fixed time intervals allow (among other things) magnetization transfer between nuclei and, therefore, the detection of the kinds of nuclear–nuclear interactions that allowed for the magnetization transfer. Interactions that can be detected are usually classified into two kinds. There are through-bond and through-space interactions.

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Sources: en.wikipedia.org

Frequently asked questions

How does CJC-1295 differ from modified GRF(1-29)?

The two share the same 29-amino-acid backbone. CJC-1295 carries an additional albumin-binding moiety that markedly extends its residence time in circulation, while the form without that moiety clears faster. Literature sometimes applies the name loosely to either variant.

Is CJC-1295 an approved medicine?

It has not been approved by major regulatory agencies for any therapeutic indication. Material sold under this name is typically distributed for laboratory research only. Clinical use is not supported by large controlled trials.

What is known about its half-life?

Early human studies of the albumin-binding form reported circulation half-lives on the order of several days. The value depends on assay method and study design. Estimates for the form without the binding moiety are considerably shorter.

What is CJC-1295?

It is a synthetic peptide analogue of growth hormone-releasing hormone. Four substitutions in its sequence make it more resistant to enzymatic degradation than the natural hormone. In the version carrying a drug affinity complex, the peptide binds albumin and remains in circulation for days.

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