This is a working overview of GHRH analogue, written for readers who want more than a one-paragraph summary but less than a textbook.
This page was last updated on 2025-08-22 and is reviewed periodically as new material appears.
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.
Receptor level activity follows the canonical GHRH pathway. The peptide binds the GHRH receptor, a class B G protein coupled receptor on somatotroph cells of the anterior pituitary. Binding raises intracellular cyclic AMP, which promotes calcium entry and the release of growth hormone into the bloodstream. Because the molecule acts at the same receptor as the endogenous hormone, its effect is superimposed on the natural pulsatile rhythm rather than replacing it. Whether sustained receptor occupation leads to desensitization is not fully settled.
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.
| Property | Value | Notes |
|---|---|---|
| Peptide class | Synthetic GHRH analogue | Built on a 29 residue sequence |
| Primary target | GHRH receptor (GHRHR) | Class B G protein coupled receptor |
| Unconjugated half life | Minutes | Limited by protease degradation |
| Key modification | Four residue substitutions | Positions 2, 8, 15 and 27 |
| Common synonym | Modified GRF(1-29) | Usually denotes the form without DAC |
Binding of the peptide to the growth hormone-releasing hormone receptor on pituitary somatotrophs triggers a G protein coupled cascade that raises cyclic AMP and opens calcium channels. The result is greater secretion of growth hormone into the bloodstream. Because the peptide acts at the same receptor as the natural hypothalamic hormone, its effect is amplified pulse size rather than an entirely separate release pathway. Receptor binding alone does not determine the response, since somatostatin tone and other inputs modulate the final output.
The albumin-binding version stays in circulation for days, because covalent attachment to serum albumin shields the peptide from rapid filtration and degradation. Reported half-lives for this form fall in the range of several days. The version without the linker is cleared in minutes, with estimates often near thirty minutes in animal work. These figures come from small studies and vary with assay method, species, and route, so they are best read as approximate rather than fixed constants.
Studies in this area generally track growth hormone pulses, insulin-like growth factor 1 concentrations, and occasionally body composition endpoints. Most published human data come from early, small trials, and questions about long-term effects remain open. Whether repeated exposure alters pituitary responsiveness over time is not settled. Analytical work relies on immunoassays for the hormones and on mass spectrometry for the peptide itself, because the two measurements answer different questions.
CJC-1295 acts at the growth hormone-releasing hormone receptor, a G-protein-coupled receptor found on somatotroph cells in the anterior pituitary. Binding triggers a rise in cyclic AMP and calcium entry, which promotes release of stored growth hormone. Because the peptide mimics the body's own releasing hormone, it amplifies existing secretory pulses rather than driving continuous output. The size of the response therefore depends partly on the subject's own hormonal rhythm and feedback state.
The attached maleimide group explains the unusual duration of the DAC version. After injection it reacts with the thiol of cysteine-34 on serum albumin, forming a stable covalent bond. The resulting conjugate is too large for rapid kidney filtration and is shielded from many peptidases. Reported half-lives for this form reach several days, whereas the version without the group is cleared in roughly half an hour. That gap is the main pharmacological difference between the two.
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.
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General technique for NPWT is as follows: A dressing or filler material is fitted to the contours of a wound to protect the periwound and the overlying foam or gauze is then sealed with a transparent film. A drainage tube is then connected to the dressing through an opening of the transparent film. Tubing is connected through an opening in the film drape to a canister on the side of a vacuum pump. This turns an open wound into a controlled, closed wound with an airtight seal while removing excess fluid from the wound bed to enhance circulation and remove wound fluids. This creates a moist healing environment and reduces edema. There are four types of dressings used over the wound surface: foam or gauze, a transparent film, and a non-adherent (woven or non-woven) contact layer if necessary. Foam dressings or woven gauze are used to fill open cavity wounds. Foam can be cut to size to fit wounds. Once the wound is filled, then a transparent film is applied over the top to create a seal around the dressing. The tubing is then attached and connected to the pump. Once the dressing is sealed, the vacuum pump can be set to deliver continuous or intermittent pressures, with levels of pressure depending on the device used, varying between −200 and −40 mmHg depending on the material used and patient tolerance. Pressure can be applied constantly or intermittently. The dressing type used depends on the type of wound, clinical objectives and patient.
Sources: en.wikipedia.org
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Specifically, carboxamides and oximes can be converted to nitriles by dehydration (elimination of water). Numerous reagents and methodologies are available for this transformation. Methods for nitrile synthesis via dehydration of nitroalkanes have also been described. Phosphorus pentoxide, known since the mid-19th century, is a classical reagent for amide dehydration. Amides can also be dehydrated using trivalent phosphorus reagents such as phosphorus trichloride or triphenyl phosphite; as well as diethyl chlorophosphate, thionyl chloride, or phosgene. In the presence of specific palladium complexes or other suitable catalysts, acetonitrile can function as a dehydrating agent, converting an amide into a nitrile while being transformed into acetamide. Similarly, dichloroacetonitrile may be employed. Related systems utilize iron(II) chloride tetrahydrate, zinc trifluoromethanesulfonate, or uranyl nitrate as catalysts in combination with N-methyl-N-trimethylsilyltrifluoroacetamide as the dehydrating reagent. Carboxylic acid amides can also be dehydrated using a system comprising triphenylphosphane, iodine, and 4-methylmorpholine. Another approach involves high-temperature dehydration (220–240 °C) in hexamethylphosphoramide (HMPA). Dehydration of primary amides with zinc chloride under microwaves is reversible. In aqueous acetonitrile, an amide can be converted to a nitrile; however, in a water–tetrahydrofuran system with added acetamide, the reverse conversion of nitrile to amide occurs.
Sources: en.wikipedia.org
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Sources: en.wikipedia.org
The names are often used interchangeably in casual writing, but they are not strictly identical. Modified GRF(1-29) refers to the unconjugated analogue carrying only the four substitutions. The version sold as CJC-1295 with DAC includes the albumin binding linker and clears much more slowly.
DAC stands for drug affinity complex, a term describing the maleimidopropionic acid linker. This group forms a covalent bond with the cysteine residue on serum albumin after administration. The resulting adduct is what extends the circulating half life from minutes to days.
No. It is entirely synthetic and does not correspond to any known endogenous peptide. The design starts from human growth hormone releasing hormone and introduces deliberate substitutions. Any biological effect comes from mimicking the natural hormone at its receptor.
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.