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Molecular Background And Naming — Background and Details

By Editorial Desk · published 2026-05-21 · last reviewed 2026-07-03 · Topic

The short version of GRF(1-29) fits in a sentence. The long version — which is the one that helps — is below.

Reviewed 2026-07-03. Anything still debated is marked as such rather than presented as settled.

Molecular Background and Naming

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.

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.

Identity and Naming History

The peptide backbone corresponds to GRF(1-29), the first 29 residues of native growth hormone-releasing hormone, which retains most of the receptor-activating activity of the full-length molecule. Four substitutions distinguish the analog from the natural sequence: D-alanine at position 2, glutamine at position 8, alanine at position 15, and leucine at position 27. These changes slow cleavage by dipeptidyl peptidase IV, the enzyme that degrades native hormone in plasma within minutes. The outcome is improved enzymatic stability combined with a still brief residence time when no additional modification is present.

Naming in this area is inconsistent, and readers should treat product labels with care. In much of the literature and in vendor catalogs, the unqualified term refers to the albumin-binding version, while the version lacking the DAC group appears as modified GRF(1-29), mod GRF(1-29), or the same name with a without-DAC qualifier. Because one abbreviation has been applied to both materials, the only reliable way to identify a sample is to check the stated sequence and the presence of the linker.

Cjc-1295 at a glance

PropertyValueNotes
Molecular weight (no linker)~3.37 kDaCalculated from peptide sequence
Molecular weight (with linker)~3.65 kDaIncludes albumin-binding moiety
AppearanceWhite to off-white powderTypically lyophilized
SolubilitySoluble in waterAlso dissolves in aqueous buffers
Common synonymsModified GRF(1-29), DAC:GRFUsage varies by source

Background and Receptor Mechanism

At the pituitary, the peptide binds the growth hormone-releasing hormone receptor on somatotroph cells. Receptor activation raises intracellular cyclic AMP and triggers release of stored growth hormone. Somatostatin and other hypothalamic signals modulate this response. Negative feedback from insulin-like growth factor 1 also influences output. The same regulatory architecture operates with the native hormone. Whether the synthetic analog alters feedback dynamics over repeated exposure remains an open question. Most published receptor work uses cell models rather than intact human systems.

CJC-1295 is a synthetic peptide belonging to the growth hormone-releasing hormone analog family. It comprises twenty-nine amino acid residues derived from the N-terminal region of natural GHRH. The molecule incorporates several non-natural substitutions that increase resistance to enzymatic degradation. These modifications extend its activity compared with the native hormone fragment. Researchers use it to study pituitary growth hormone secretion in laboratory and clinical settings. This compound is distinct from native GHRH in its stability profile.

Two principal forms appear in the literature and in research supply. One carries a drug affinity complex, a maleimide-based group that forms a covalent bond with circulating albumin. This linkage slows clearance and produces a long-lasting elevation of peptide levels. The other form lacks that group and is often labeled MOD GRF(1-29). It has a much shorter circulation time. Both variants retain the same core receptor-binding sequence. Reported half-lives differ substantially between the two.

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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.

Structure And Receptor Pharmacology

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 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.

Background from the literature

==== Modifications of translation factors ==== diphthamide formation (on a histidine found in eEF2) ethanolamine phosphoglycerol attachment (on glutamate found in eEF1α) hypusine formation (on conserved lysine of eIF5A (eukaryotic) and aIF5A (archaeal)) beta-Lysine addition on a conserved lysine of the elongation factor P (EFP) in most bacteria. EFP is a homolog to eIF5A (eukaryotic) and aIF5A (archaeal) (see above).

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Sources: en.wikipedia.org

Further detail

Valdecoxib is a nonsteroidal anti-inflammatory drug (NSAID) used in the treatment of osteoarthritis, rheumatoid arthritis, and painful menstruation and menstrual symptoms. It is a selective cyclooxygenase-2 inhibitor. It was patented in 1995. Valdecoxib was manufactured and marketed under the brand name Bextra by G. D. Searle & Company as an anti-inflammatory arthritis drug. It was approved by the United States Food and Drug Administration (FDA) on November 20, 2001, to treat arthritis and menstrual cramps, and was available by prescription in tablet form until 2005 when the FDA requested that Pfizer (Searle's parent company) withdraw Bextra from the American market. The FDA cited "potential increased risk for serious cardiovascular (CV) adverse events," an "increased risk of serious skin reactions" and the "fact that Bextra has not been shown to offer any unique advantages over the other available NSAIDs." In 2009, Bextra was at the center of the "largest health-care fraud settlement and the largest criminal fine of any kind ever." Pfizer paid a $2.3 billion civil and criminal fine. Pharmacia & Upjohn, a Pfizer subsidiary, violated the United States Food, Drug and Cosmetic Act for misbranding Bextra "with the intent to defraud or mislead." A water-soluble and injectable prodrug of valdecoxib, parecoxib, is marketed in the European Union under the tradename Dynastat.

Demoxytocin (INN; brand names Sandopart, Odeax, Sandopral; also known as desaminooxytocin, deaminooxytocin, 1-(3-mercaptopropanoic acid)oxytocin, and [Mpa1]OT) is an oxytocic peptide drug that is used to induce labor, promote lactation, and to prevent and treat puerperal (postpartum) mastitis (breast inflammation). Demoxytocin is a synthetic analogue of oxytocin and has similar activities, but is more potent and has a longer half-life in comparison. Unlike oxytocin, which is given via intravenous injection, demoxytocin is administered as a buccal tablet formulation. The drug was first synthesized in 1960 and was introduced into clinical practice in 1971 by Sandoz. It is marketed in several European countries, including Italy, Czech Republic, and Poland. It has the amino acid sequence Mpa-Tyr-Ile-Gln-Asn-Cys-Pro-Leu-Gly-NH2 (Mpa = β-mercaptopropionic acid), and is an analogue of oxytocin wherein the leading cysteine is replaced with β-mercaptopropionic acid.

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Sources: en.wikipedia.org

Supporting material

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Alcohol dehydrogenases (ADH) (EC 1.1.1.1) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+) to NADH. In humans and many other animals, they serve to break down alcohols that are otherwise toxic, and they also participate in the generation of useful aldehyde, ketone, or alcohol groups during the biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+.

Sources: en.wikipedia.org

Frequently asked questions

Is CJC-1295 a natural hormone?

No. It is a synthetic analogue modeled on the first 29 residues of human GHRH. The substitutions and any linker are laboratory modifications rather than features of the endogenous peptide.

Why do two versions share one name?

Early development used the albumin-binding form, and a shorter variant was later discussed under the same label. Because the two differ in half-life and handling, ambiguity arises whenever a source omits the variant designation.

What is the relationship to GRF(1-29)?

The compound derives from that fragment but is not identical to it. The parent fragment lacks the stabilizing substitutions, so its degradation rate and duration of action differ noticeably.

Is this compound a naturally occurring hormone?

No. It is a laboratory-made analog of growth hormone-releasing hormone. The natural hormone is a 44-residue peptide, while the analog is built on a shorter 29-residue fragment.

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