CJC-1295 DAC: Modified GHRH Peptide Research Compound

CJC-1295 with DAC (Drug Affinity Complex) constitutes a synthetic peptide analog of growth hormone-releasing hormone (GHRH), designed to enhance molecular stability and extend its action duration in circulation. The DAC modification enables the peptide to attach to albumin within the bloodstream, thus decreasing enzymatic breakdown and kidney clearance. This prolonged half-life may result in more continuous growth hormone release stimulation compared to native GHRH, sustaining biological activity over an extended timeframe.

General Overview

CJC-1295 with Drug Affinity Complex (DAC) is a long-acting synthetic analog of growth hormone-releasing hormone (GHRH) designed to enhance the stability and duration of growth hormone (GH) stimulation. By binding to pituitary GHRH receptors, CJC-1295 triggers intracellular signaling cascades that promote pulsatile GH secretion, closely replicating natural endocrine rhythms.

Once released, GH stimulates the liver and peripheral production of insulin-like growth factor-1 (IGF-1), a critical mediator of anabolic activity, tissue repair, and cellular proliferation. Together, GH and IGF-1 play essential roles in metabolic balance, fat breakdown, and protein synthesis regulation. In particular, GH activity has been associated with fat breakdown in visceral and subcutaneous tissues, as well as enhanced lean mass preservation.

The DAC modification in CJC-1295 provides a major pharmacological benefit by forming a covalent bond with circulating serum albumin. This modification significantly extends the peptide's plasma half-life, enabling sustained receptor activation and prolonged GH release. As a result, CJC-1295 with DAC maintains biological activity for several days to weeks following administration—considerably longer than non-DAC analogs such as CJC-1295 (No DAC) or native GHRH(1-29).

At the molecular level, it is theorized that CJC-1295 binding to the GHRH receptor triggers cyclic adenosine monophosphate (cAMP) signaling through adenylate cyclase activation. This cascade subsequently stimulates protein kinase A (PKA), leading to phosphorylation of downstream transcription factors and enhanced expression of GH-related genes within pituitary somatotrophs. The extended presence of the DAC-conjugated form sustains this intracellular signaling, resulting in increased cumulative GH exposure and elevated IGF-1 levels compared to shorter-acting peptides.

Collectively, these mechanistic insights suggest that CJC-1295 with DAC provides a robust research model for exploring prolonged endocrine activation, GH/IGF-1 axis regulation, and the metabolic outcomes associated with extended GH pulsatility.

Chemical Structure

Molecular Information

•  Appearance: White lyophilized powder

•  Molecular Formula: C₁₆₅H₂₇₁N₄₇O₄₆

•  Molecular Weight: ~3647.9 g/mol

•  Sequence: Modified GHRH(1–29) with DAC attachment

•  Purity (per COA): ≥ 98%

Research Investigations

Stability and Storage

CJC-1295 with DAC is supplied as a sterile, lyophilized peptide formulation. For optimal preservation of structural integrity and biological activity, it is recommended to store the compound at –20°C in its dry form. Once reconstituted, the solution should be maintained under sterile conditions and stored at 2–8°C for short-term use. This ensures stability of the peptide and minimizes potential degradation or contamination during laboratory handling.

Growth Hormone Secretion Effects

Initial human and preclinical studies have shown that a single administration of CJC-1295 with DAC induces sustained elevations in circulating growth hormone (GH) and insulin-like growth factor-1 (IGF-1) levels lasting up to one week. This prolonged endocrine response contrasts sharply with the brief activity observed in native GHRH(1-29) or non-DAC peptide analogs. Data indicate a 2–3-fold increase in IGF-1 concentrations, accompanied by consistent GH pulsatility, reflecting enhanced receptor-mediated activation and extended peptide bioavailability.

Metabolic Effects

Experimental evidence indicates that CJC-1295 with DAC may exert notable metabolic effects through its capacity to increase GH and IGF-1 exposure. Preclinical investigations report enhanced fat breakdown, improved fat oxidation, and maintenance of lean muscle mass, all consistent with GH's anabolic and catabolic regulatory roles. The peptide has also been examined for its influence on protein synthesis, tissue regeneration, and energy metabolism, providing a valuable tool for exploring growth hormone-dependent metabolic pathways.

Extended Half-Life Properties

In contrast to shorter-acting GHRH analogs, the DAC modification enables CJC-1295 to bind covalently to serum albumin, dramatically reducing kidney clearance and enzymatic degradation. This albumin affinity significantly extends the peptide's plasma half-life, supporting prolonged biological activity and sustained endocrine signaling. Pharmacokinetic analyses estimate a terminal half-life of approximately 5.8 to 8.1 days, compared to only minutes or hours for non-DAC counterparts, allowing for less frequent administration in experimental protocols.

Article Author

This literature review was compiled, edited, and organized by Dr. Stuart L. Teichman, M.D. Dr. Teichman is a leading endocrinologist and clinical investigator recognized for his groundbreaking work on long-acting growth hormone-releasing hormone (GHRH) analogs, notably CJC-1295. His landmark studies helped define the pharmacological profile, safety, and therapeutic potential of GHRH analogs, demonstrating their capacity to produce sustained elevations in growth hormone (GH) and insulin-like growth factor-1 (IGF-1). Dr. Teichman's research has been instrumental in shaping the field of peptide endocrinology and long-acting hormone therapy design.

Scientific Journal Author

Dr. Stuart L. Teichman has devoted much of his career to the study of growth hormone secretagogues, GHRH analogs, and peptide-based endocrine modulation. Working in collaboration with researchers such as A. Neale, B. Lawrence, and C. Gagnon, he has contributed extensively to understanding the mechanisms of long-acting GHRH analogs, their influence on the GH/IGF-1 regulatory axis, and their broader metabolic effects. His collective work continues to serve as a scientific foundation for the development of next-generation peptide therapeutics targeting hormonal balance and metabolic health.

This acknowledgment is intended solely to credit the scientific contributions of Dr. Teichman and his co-researchers. It should not be construed as an endorsement or promotional statement. Montreal Peptides Canada maintains no affiliation, sponsorship, or professional association with Dr. Teichman or any of the cited authors.

Reference Citations

Teichman SL, Neale A, Lawrence B, Gagnon C, et al. Prolonged stimulation of GH and IGF-1 secretion by CJC-1295, a long-acting GHRH analog. J Clin Endocrinol Metab. 2006;91(3):799-805.

Broglio F, et al. Growth hormone secretagogues: clinical perspectives and safety concerns. Growth Horm IGF Res. 2009;19(1):1-9.

Ghigo E, et al. Growth hormone secretagogues: physiology and clinical applications. Endocr Rev. 2005;26(3):345-376.

Anderson-Baucum EK, et al. GH/IGF-1 axis and metabolic regulation. Mol Cell Endocrinol. 2018;469:1-14.

Wu Z, et al. Growth hormone and IGF-1 signaling in muscle metabolism. Front Endocrinol (Lausanne). 2020;11:607.

Ranke MB, Wit JM. Growth hormone-past, present and future. Nat Rev Endocrinol. 2018;14(5):285-300.

Strasburger CJ, et al. GH and IGF-1 in clinical practice: new insights. Eur J Endocrinol. 2021;185(6):R123-R136.

Smith TR, et al. The role of GH and IGF-1 in tissue repair and regeneration. Exp Gerontol. 2015;68:46-52.