The short version of DAC group fits in a sentence. The long version — which is the one that helps — is below.
This page was last updated on 2026-03-28 and is reviewed periodically as new material appears.
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.
CJC-1295 is the name used for a synthetic peptide modeled on growth hormone-releasing hormone, the hypothalamic signal that prompts the pituitary to release growth hormone. The compound was described by a Canadian drug discovery company in the mid-2000s as a long-acting research tool. Two closely related molecules share the name in practice: one carries a drug affinity complex, or DAC, group, and one does not. The distinction matters because the two behave differently in circulation.
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.
| Property | Value | Notes |
|---|---|---|
| Molecular class | Synthetic peptide | GHRH analog, not a steroid |
| Backbone length | 29 amino acids | Based on GRF(1-29) |
| Substitutions | Four positions | D-Ala2, Gln8, Ala15, Leu27 |
| Appearance | White to off-white powder | Typical lyophilized research material |
| Common synonyms | Modified GRF(1-29) | Usage varies between sources |
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.
Reverse-phase high-performance liquid chromatography is the standard tool for purity assessment. The technique separates the target peptide from truncated or modified byproducts. Mass spectrometry confirms molecular weight and supports sequence verification. Electrospray ionization and matrix-assisted laser desorption are both used. Amino acid analysis provides an independent check on composition. Purity values are commonly reported as area percentage from the chromatogram. Residual trifluoroacetate and water content are also measured in many quality programs.
Batch-to-batch consistency depends on solid-phase peptide synthesis and subsequent purification. Coupling efficiency, resin choice, and cleavage conditions all affect the final profile. Counter-ion content and moisture can shift the apparent mass of a batch. Documentation typically includes a certificate of analysis with chromatograms and spectra. Independent verification by a second laboratory is sometimes requested. Whether a given certificate reflects the actual vial contents depends on chain of custody. Analytical methods themselves carry uncertainty that should be stated alongside results.
== Chemistry == Proteins constitute 90-95% of venom's dry weight and are responsible for almost all of its biological effects. The hundreds, even thousands, of proteins found in venom include toxins, neurotoxins in particular, as well as nontoxic proteins (which also have pharmacological properties), and many enzymes, especially hydrolytic ones. Enzymes (molecular weight 13-150 KDa) make up 80-90% of viperid and 25-70% of elapid venoms, including digestive hydrolases, L-amino-acid oxidase, phospholipases, thrombin-like pro-coagulant, and kallikrein-like serine proteases and metalloproteinases (hemorrhagins), which damage vascular endothelium. Polypeptide toxins (molecular weight 5-10 KDa) include cytotoxins, cardiotoxins, and postsynaptic neurotoxins (such as α-bungarotoxin and α-Cobratoxin), which bind to acetylcholine receptors at neuromuscular junctions. Compounds with low molecular weight (up to 1.5 KDa) include metals, peptides, lipids, nucleosides, carbohydrates, amines, and oligopeptides, which inhibit angiotensin-converting enzyme (ACE) and potentiate bradykinin (BPP). Inter- and intra-species variation in venom chemical composition is geographical and ontogenic. Phosphodiesterases interfere with the prey's cardiac system, mainly to lower the blood pressure. Phospholipase A2 causes hemolysis by lysing the phospholipid cell membranes of red blood cells. Amino acid oxidases and proteases are used for digestion. Amino acid oxidase also triggers some other enzymes and is responsible for the yellow colour of the venom of some species.
From a scientific standpoint, it was a well characterized protein, whose structure had already been elucidated, making it easier to work with, in theory. Additionally, the widely available insulin at the time was pig insulin, and many people presented allergic reactions to this insulin. Human insulin, then, was preferable, for it was believed that people would not have allergic reactions to it. From a business standpoint, there was a large market for insulin; at the time, world sales were greater than $100 million, and growing. Boyer agreed that the insulin hormone should be their first target molecule. After concluding the market research, Swanson prepared Genentech's first business proposal by March 1976. It was with this proposal that Swanson pitched Genentech to Kleiner & Perkins. Perkins later explained that they considered the technical risks to be enormous: "(The risk of failure was) Very high. I figured better than 50–50 we'd lose it... (However) If it worked, the rewards would be obvious.". Boyer's scientific expertise and Swanson's business plan convinced the venture capitalists. While acknowledging the tremendous risk associated with the company, Kleiner and Perkins promised to invest $100,000 in Genentech. This was just a small fraction of Kleiner and Perkins's $8 million venture capital fund.
=== United States === Zinc pyrithione concentration of up to 2% is allowed for products when they are formulated to be applied and then washed off after brief exposure. Alternatively, up to 0.25 percent when formulated to be left on the skin or scalp
Sources: en.wikipedia.org
=== 1967–1968: RoBee's and Marriott === In 1967, the Azar's Big Boy restaurant franchise started RoBee's House of Beef restaurants in Ft. Wayne, Indiana. The Marriott Corp., which had acquired Bob's Big Boy and the Big Boy trademark in 1967, acquired RoBee's in February 1968 with plans to expand nationwide. RoBee's franchises would first be offered to Big Boy franchisees to coincide with their existing Big Boy territory. At the time there were 13 RoBee's restaurants in six states. During the acquisition, in January 1968, the competing roast beef chain Arby's sued RoBee's for trademark infringement and (other similarities that it considered) unfair competition. Because "RoBee's" sounded too much like "Arby's" the settlement required a new brand name and Marriott wanted something recognizable. Big Boy founder Bob Wian, then sitting on Marriott's board of directors, was friends with Roy Rogers' agent and suggested that the company approach Rogers about the use of his name. Already interested in associating with a chain restaurant, Rogers was in similar discussions with another company when Marriott called. Nonetheless, he accepted Marriott's offer: Rogers would receive a licensing fee for use of his name and also be paid for personal appearances at the restaurants. The restaurants would be called "Roy Rogers Roast Beef Sandwich" restaurants, and despite Arby's complaints, it retained RoBee's building design and covered wagon logo design.
Catching a chameleon: mRNA can be engineered to overcome cancer evolution, essay by Elias Sayour, a pediatric oncologist. Science (journal), 2 Apr 2026 "Five things you need to know about: mRNA vaccines". Horizon. Archived from the original on 4 April 2020. Retrieved 17 November 2020. "RNA vaccines: an introduction". PHG Foundation. University of Cambridge. "Understanding mRNA COVID-19 Vaccines". Centers for Disease Control and Prevention. 4 January 2022. Kolata G, Mueller B (15 January 2022). "Halting Progress and Happy Accidents: How mRNA Vaccines Were Made". The New York Times. M.I.T. Lecture 10: Kizzmekia Corbett, Vaccines" on YouTube
== Application == Due to the hemolytic toxicity of Guanacastepene A, it is not currently used directly in human clinical medicine. Its main potential, however, lies in its function as a "resistance breaker" against antibiotic-resistant pathogens, as various experiments have demonstrated its efficacy against methicillin-resistant Staphylococcus aureus (MRSA) and vancomycin-resistant Enterococcus faecalis (VRE). Furthermore, a more specific area of application arises in antifungal research, as newly isolated members of the guanacastane family, such as guanacastepene V, isolated from the marine fungus Coprinellus xanthothrix discovered on the surface of a barnacle off the coast of Japan (Kashima City), exhibit a selective effect against the yeast Candida auris. This species is considered an emerging multidrug-resistant yeast. Although guanacastepene V inhibits the growth of Candida auris with an MIC of 6.25 µg/ml, it also exhibits high selectivity, as it has virtually no effect on Candida albicans at an MIC of 100 µg/ml. Therefore, opportunities may arise to further develop other members of the guanacastane family to combat Candida albicans outbreaks in hospitals. Guanacastepene A also serves as a challenging target molecule for total chemical synthesis, making it useful for developing and testing novel synthetic methods; examples include the controlled fragmentation of cyclobutane rings or innovative variants of the Robinson annulation reaction for constructing complex seven-membered ring systems.
Sources: en.wikipedia.org
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.
The original material included a linker that binds serum albumin. A later variant removed that linker to reduce the duration of action. Catalogs and papers did not consistently adopt separate names, so both remain widely labeled with the same term.
The amino acid sequence and the presence or absence of the linker group. Mass measured by spectrometry gives an independent check that separates the two forms.
It binds the growth hormone-releasing hormone receptor on pituitary somatotroph cells. Receptor activation raises cyclic AMP and promotes release of stored growth hormone granules. Because the peptide persists longer than natural releasing hormone, stimulation is prolonged rather than brief.