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Cjc-1295 Structure And Mechanism — Quick Reference

By Editorial Desk · published 2025-12-10 · last reviewed 2025-12-29 · News

drug affinity complex raises a handful of sensible questions. This page answers them in order, starting with the fundamentals and moving to applications.

Reviewed 2025-12-29. Anything still debated is marked as such rather than presented as settled.

CJC-1295 Structure And Mechanism

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.

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.

Compound Identity and Development History

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.

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

Characterization of this peptide relies on a small set of routine techniques. Reversed-phase high-performance liquid chromatography separates the target from truncated or oxidized by-products and yields a purity estimate when paired with ultraviolet detection near 214 nanometers. Mass spectrometry, either electrospray coupled to liquid chromatography or matrix-assisted laser desorption, confirms that the observed mass matches the value calculated for the expected sequence. Amino acid analysis, and enzymatic digestion followed by fragment mapping, are used when the sequence itself rather than the mass requires verification.

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.

Structure And Receptor Pharmacology

CJC-1295 belongs to a class of synthetic peptides modeled on growth hormone releasing hormone, a forty-four amino acid signal produced by the hypothalamus. The compound is built from the first twenty-nine residues of the natural sequence, with four substitutions introduced at positions 2, 8, 15 and 27. These changes were designed to slow enzymatic breakdown while preserving receptor activation. The result is a peptide that is shorter than native GHRH and considerably more resistant to ordinary clearance pathways in circulation.

Two related forms appear under the CJC-1295 name. The simpler analogue, commonly written as modified GRF(1-29), carries the four substitutions but no additional conjugation. The second form attaches a maleimidopropionic acid linker to a lysine residue, a modification frequently called the drug affinity complex. That linker reacts with the free thiol on serum albumin to form a covalent bond. Because albumin has a long residence time in blood, the conjugated peptide stays in circulation far longer than the unconjugated analogue.

Background and Molecular Features

Two related peptides circulate under the CJC-1295 label, and they differ mainly in how long they persist in circulation. The version carrying a drug affinity complex includes a maleimidopropionic acid linker that forms a covalent bond with serum albumin. The other version, usually written as modified GRF(1-29) or tetrasubstituted GRF(1-29), lacks that linker and is cleared quickly. Mixing the two produces inconsistent readings of published half-life values, because the linker rather than the receptor-facing sequence drives most of the difference.

The core sequence keeps the receptor-binding region of GHRH while replacing four positions that are vulnerable to dipeptidyl peptidase-4 and other proteases. Substitutions at positions 2, 8, 15, and 27 raise metabolic stability relative to the natural hormone. The N-terminal residues remain essential for activity, so changes there generally lower potency. Molecular weight sits near 3368 daltons for the tetrasubstituted analog without the linker, while the albumin-binding form is heavier because of the added maleimide group.

Supporting material

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Since the oxychlorides are asymmetrical, and they should have increasingly large electric dipole moments going down the group, they should become less volatile in the order TcO3Cl > ReO3Cl > BhO3Cl: this was experimentally confirmed in 2000 by measuring the enthalpies of adsorption of these three compounds. The values are for TcO3Cl and ReO3Cl are −51 kJ/mol and −61 kJ/mol respectively; the experimental value for BhO3Cl is −77.8 kJ/mol, very close to the theoretically expected value of −78.5 kJ/mol.

== Distribution and habitat == Panaeolus cyanescens is a coprophilous (dung-inhabiting) species which occurs in both the Neotropics and Paleotropics. It has been found in Vietnam, Africa (including South Africa, Mauritius, Madagascar and Democratic Republic of the Congo), Australia, Belize, the Caribbean (Bermuda, Grenada, Barbados Jamaica, Trinidad, and Puerto Rico), Costa Rica, India, Malaysia, Indonesia, Sri Lanka, Cambodia, Thailand, Japan, Mexico, Oceania (Fiji and Samoa), the Philippines, South America (Bolivia, Brazil, Paraguay, Colombia, Venezuela, and Ecuador), South Korea, and the United States (California, Hawaii, Louisiana, Mississippi, Alabama, Florida, Tennessee, Texas, Kentucky, Virginia, Georgia, and North Carolina).

Sources: en.wikipedia.org

Supporting material

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Sources: en.wikipedia.org

Supporting material

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== Role in development == Knockout mice with the Ctgf gene disrupted die at birth due to respiratory stress as a result of severe chondrodysplasia. Ctgf-null mice also show defects in angiogenesis, with impaired interaction between endothelial cells and pericytes and collagen IV deficiency in the endothelial basement membrane. CTGF is also important for pancreatic beta cell development and is critical for normal ovarian follicle development and ovulation.

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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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