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CJC-1295 DAC is a synthetic peptide analogue, modified by the inclusion of a maleimide-based Drug Affinity Complex (DAC), which has been studied as a well-defined molecular compound in controlled laboratory research.
CJC-1295 DAC is a synthetic peptide analogue of growth hormone-releasing hormone (GHRH) developed for experimental investigation of GHRH receptor pharmacology and peptide stability. It is a modified GHRH-derived peptide containing 30 amino acid residues and incorporates several amino acid substitutions designed to alter the physicochemical and enzymatic properties of the native peptide. The designation DAC refers to a Drug Affinity Complex, a chemical modification that enables covalent interaction with circulating albumin.
CJC-1295 was developed by ConjuChem as part of research into extending the persistence of peptide compounds through albumin-binding technology. The DAC-containing form incorporates a reactive maleimide-containing linker attached to a lysine residue. Published studies have characterised the resulting conjugation with albumin and investigated how this modification alters the peptide’s pharmacokinetic behaviour compared with unmodified GHRH-derived peptides.
Within laboratory research, CJC-1295 DAC is recognised principally for investigations of GHRH receptor interactions, peptide–protein conjugation, albumin binding, peptide degradation and pharmacokinetics. Its molecular characteristics can be examined using chromatographic and mass-spectrometric techniques, while receptor-mediated signaling is investigated using biochemical and cell-based assays.
CJC-1295 DAC should be distinguished from CJC-1295 without DAC, often informally called Modified GRF (1–29), because the two compounds differ structurally and should not be treated as interchangeable research materials.
A synthetic 30-amino acid peptide that mimics growth hormone-releasing hormone (GHRH) is called CJC-1295 DAC. The biologically active N-terminal region of GHRH serves as the foundation for its main structure. It retains structural characteristics linked to GHRH receptor recognition while including amino acid alterations meant to alter sensitivity to enzymatic breakdown. The Drug Affinity Complex (DAC) alteration, which includes a reactive maleimide-containing group connected by a lysine side chain, is a distinguishing structural feature.
The peptide is a linear, relatively hydrophilic molecule containing a mixture of acidic, basic, polar and non-polar amino acid residues. Its ionization state and net charge therefore vary with pH and the composition of the experimental buffer. As a short peptide, CJC-1295 DAC does not possess the stable tertiary architecture characteristic of larger proteins, although local secondary conformations may occur in solution or during receptor interaction.
The DAC modification sets CJC-1295 DAC apart from GHRH analogs that are not DAC. A covalent peptide–albumin combination can be created when its maleimide activity combines with a free thiol group on serum albumin. This structural alteration has been studied as a way to change the stability and clearance susceptibility of peptides.
CJC-1295 DAC is generally supplied in lyophilized form for laboratory applications. Its physicochemical integrity can be affected by moisture, temperature, pH and enzymatic exposure following reconstitution. Analytical HPLC and mass spectrometry are commonly used to characterize purity, molecular identity and DAC-containing peptide preparations.
As a modified analog of growth hormone-releasing hormone (GHRH) intended to interact with the growth hormone-releasing hormone receptor (GHRHR), CJC-1295 DAC has been studied in recent studies. According to published experimental research, GHRHR is a class B G protein-coupled receptor (GPCR), and CJC-1295 retains the structural characteristics of GHRH necessary for receptor activation and recognition.
Following ligand–receptor interaction, GHRHR has been characterised as coupling predominantly to the stimulatory G protein Gαs. This interaction activates adenylyl cyclase, leading to intracellular creation of cyclic adenosine monophosphate (cAMP) and cAMP-dependent protein activation that follows kinase A (PKA). Laboratory studies of GHRH receptor signaling have used receptor-binding experiments, cAMP assays, and cell-based systems to characterize this pathway and associated downstream phosphorylation events.
A distinguishing mechanistic feature of CJC-1295 DAC is its Drug Affinity Complex (DAC). The peptide contains a reactive maleimide-containing moiety that has been investigated for its ability to form a covalent bond with a free thiol, particularly cysteine-34 of serum albumin. Published experimental studies describe this albumin conjugation as altering the peptide's pharmacokinetic behavior and protecting the peptide component from processes associated with rapid enzymatic degradation and renal clearance. Albumin binding therefore represents a pharmacokinetic modification rather than a separate receptor-mediated signaling mechanism.
The resistance of modified GHRH analogs to dipeptidyl peptidase IV (DPP-IV/DPP-4), an enzyme responsible for the quick breakdown of native GHRH, has also been investigated experimentally. Changes in enzymatic susceptibility have been described in relation to amino acid changes included in CJC-1295.
In general, the process being studied combines DAC-dependent albumin conjugation with GHRHR-mediated signal transduction. In order to understand how structural alteration affects receptor interaction, peptide stability, and molecular persistence, these processes have been investigated utilizing receptor pharmacology, biochemical tests, and pharmacokinetic models.
This is based on findings recorded in published preclinical and in vitro literature, with main studies listed in the references.
CJC-1295 DAC has been investigated in relation to the growth hormone-releasing hormone receptor (GHRHR), a class B G protein-coupled receptor. Experimental research has examined ligand–receptor recognition, receptor activation and G-protein-mediated signal transduction using receptor-binding assays and cell-based expression systems.
A research area particularly relevant to CJC-1295 DAC concerns its Drug Affinity Complex technology. Studies have characterised the reactive maleimide-containing group and its capacity to form a covalent conjugate with serum albumin, particularly through albumin cysteine-34. This provides an experimental model for investigating how protein conjugation modifies the molecular behaviour of peptide analogues.
To comprehend the enzymatic mechanisms underlying peptide breakdown, modified GHRH analogs have been studied. Proteolytic enzyme susceptibility, such as dipeptidyl peptidase IV (DPP-IV/DPP-4), and the impact of amino acid changes on peptide stability have been studied in relation to CJC-1295.
Laboratory studies of CJC-1295 and GHRH-derived peptides have examined intracellular signaling associated with GHRHR activation. Particular attention has been given to Gαs-mediated adenylyl cyclase activity, intracellular cyclic AMP (cAMP) formation and protein kinase A (PKA)-associated signaling using biochemical and cell-based assays.
CJC-1295 DAC has been investigated as a model for studying the pharmacokinetic consequences of covalent albumin association. Experimental studies have characterised peptide–albumin conjugation, circulating molecular species, clearance behaviour and the persistence of DAC-modified peptides compared with shorter-acting GHRH analogues.
Peptide chemistry research has examined how individual amino acid substitutions and chemical modifications influence GHRH analogue stability, receptor recognition and molecular properties. CJC-1295 DAC provides a useful experimental construct for investigating the relationship between peptide sequence, DAC modification and biochemical behaviour.
Distinguishing intact CJC-1295 DAC, synthesis-related contaminants, and peptide–albumin conjugates are the main goals of analytical study. Under regulated laboratory circumstances, molecular identity, purity, conjugation, and stability can be investigated using techniques including LC–MS and HPLC, and complementary protein analytical methods.
CJC-1295 DAC is a synthetic modified peptide typically produced using Solid Phase Peptide Synthesis (SPPS), followed by incorporation of the Drug Affinity Complex (DAC) functionality under controlled manufacturing conditions. Following synthesis, preparative high-performance liquid chromatography (HPLC) can be used to separate the target peptide from truncated sequences, unreacted starting materials and other synthesis-related impurities.
Analytical HPLC is commonly used amongst scientists to assess chromatographic purity and batch consistency, while LC-MS verifies molecular identification and anticipated molecular mass.
Complementary identity may be obtained using other techniques like amino acid analysis or peptide mapping.
CJC-1295 DAC should be stored at 2–8°C according to the Certificate of Analysis. Keep the lyophilised material in a tightly closed container and protect it from moisture, heat, and direct light.
When handling the material, keep the container closed when not in use. Avoid leaving it exposed to room conditions for long periods. Handle it carefully in a clean laboratory setting.
DAC stands for Drug Affinity Complex. In CJC-1295 DAC, this refers to a chemical modification incorporating a reactive maleimide group designed to form a covalent conjugate with serum albumin. This modification has been investigated as a method of altering the pharmacokinetic characteristics and molecular persistence of peptide compounds.
CJC-1295 DAC contains a Drug Affinity Complex that enables covalent association with serum albumin. The compound commonly marketed as CJC-1295 without DAC is generally a modified GRF (1–29) peptide lacking the albumin-reactive group and therefore has substantially different molecular and pharmacokinetic characteristics. For scientific accuracy, the two compounds should not be treated as chemically identical research materials.
A Drug Affinity Complex is a chemical modification developed to enable a molecule to associate covalently with a circulating protein such as albumin. In CJC-1295, the DAC incorporates a maleimide functionality capable of reacting with an accessible thiol group on albumin, producing a peptide–protein conjugate that can be studied independently from the unconjugated peptide.
Published research describes CJC-1295 DAC as forming a covalent conjugate with serum albumin through its reactive maleimide-containing modification. The reaction occurs predominantly with an accessible sulfhydryl group on albumin. This albumin association has been investigated for its influence on peptide stability, distribution and clearance.
Cysteine-34 (Cys34) is the principal free cysteine residue of human serum albumin and contains a reactive thiol group. The maleimide functionality incorporated into the DAC can react with this thiol, forming a covalent peptide–albumin conjugate. Cys34 is therefore an important molecular site in studies examining DAC-based albumin conjugation.
CJC-1295 has been investigated in relation to the growth hormone-releasing hormone receptor (GHRHR). GHRHR is a class B G protein-coupled receptor (GPCR) that interacts with endogenous GHRH and initiates intracellular signalling principally through Gαs, adenylyl cyclase and cyclic AMP (cAMP)-associated pathways.
CJC-1295 incorporates substitutions within its GHRH-derived sequence that were investigated to modify susceptibility to enzymatic degradation. Of particular relevance is resistance to cleavage by dipeptidyl peptidase-4 (DPP-4/DPP-IV), an enzyme involved in the rapid N-terminal degradation of native GHRH. These sequence modifications, together with DAC-mediated albumin conjugation, have been characterised as distinct structural strategies for modifying the stability and pharmacokinetic behaviour of the peptide.
CJC-1295 DAC is provided for laboratory research and scientific investigation only. It is not for human consumption or veterinary use and is not intended for administration. It is not intended to diagnose, treat, cure, or prevent any disease or medical condition. Information on this page is provided for scientific research purposes only.
