CJC-1295 with DAC

CJC-1295 with DAC: Pharmacological Characteristics and Research Applications

CJC-1295 with DAC (Drug Affinity Complex) is a laboratory-produced peptide derived from the natural growth hormone–releasing hormone (GHRH) molecule. Through advanced chemical engineering, this compound overcomes typical stability constraints by incorporating a specialized albumin-binding domain that substantially improves resistance to degradation and extends the active duration. The DAC technology enables the peptide to bind serum albumin proteins, effectively shielding the molecule from kidney-mediated clearance and enzymatic breakdown. The outcome is a markedly extended period of GH stimulation that far surpasses the response duration achieved with conventional GHRH formulations.

Biological Mechanism and Physiological Actions

CJC-1295 modified with a Drug Affinity Complex functions as an extended-release analog of GHRH engineered to provide heightened stability and prolonged GH secretion stimulation. The peptide operates by binding to GHRH receptors on pituitary somatotroph cells, thereby triggering the intracellular processes that generate the natural pulsatile secretion pattern of GH, thereby mimicking normal circadian and ultradian rhythms.

Upon liberation from the pituitary into the bloodstream, GH acts as an endocrine signal promoting the liver and extrahepatic tissues to produce and release insulin-like growth factor-1 (IGF-1), the primary molecular mediator of anabolic responses, cellular growth, and tissue remodeling. The combined effects of GH and IGF-1 comprise the fundamental regulatory system governing nutrient metabolism, the conversion of stored fat into usable energy, and the synthesis and accumulation of muscle proteins. Particularly relevant, GH drives the hydrolysis of triglycerides within all adipose tissue compartments while simultaneously supporting the preservation of muscular tissue.

A key advantage of the DAC technology resides in the ability of the modified peptide to establish stable associations with circulating serum albumin. This interaction produces a dramatic prolongation of the peptide's presence in the bloodstream, sustaining ongoing receptor signaling and continuous GH secretion. Therefore, CJC-1295 with DAC exhibits continued biological function extending over days to weeks following administration—representing a substantial improvement over non-DAC variants like conventional CJC-1295 or native GHRH(1-29).

At the molecular level, CJC-1295 attachment to GHRH receptors is believed to activate intracellular adenylate cyclase, triggering the generation of cyclic adenosine monophosphate (cAMP). This second messenger subsequently engages protein kinase A (PKA), resulting in phosphorylation of nuclear transcription factors and augmented transcription of GH genes in pituitary cells. The continuous presence of the albumin-conjugated peptide perpetuates these biochemical signals, culminating in increased cumulative GH secretion and amplified circulating IGF-1 levels exceeding those achieved with shorter-lived peptide alternatives.

In essence, CJC-1295 with DAC represents a valuable scientific tool for investigating mechanisms of sustained endocrine stimulation, mapping the regulatory circuits of the GH/IGF-1 axis, and documenting the physiological and metabolic sequelae of extended pulsatile GH secretion.

CJC-1295 with DAC Structural and Molecular Data

Chemical Composition

Appearance: Colorless lyophilized powder

Molecular Formula: C₁₆₅H₂₇₁N₄₇O₄₆

Molecular Weight: Approximately 3647.9 g/mol

Sequence Designation: GHRH(1–29) containing covalently linked DAC

Purity: ≥ 98% per analytical documentation

CJC-1295 with DAC: Experimental Considerations and Handling

Proper Storage to Maintain Stability

CJC-1295 with DAC is distributed in sterile, lyophilized powder form suitable for laboratory research. To protect the structural integrity and functional properties throughout storage duration, the powder should be kept at –20°C in the desiccated state. Following dissolution into aqueous solution, the resulting liquid must be handled aseptically and refrigerated at 2–8°C for short-term experimental applications. Compliance with these storage specifications maintains chemical integrity and eliminates the potential for chemical degradation or biological contamination during handling procedures.

GH Secretion Induction and Duration

Studies in human subjects and animal models have shown that administration of a single dose of CJC-1295 with DAC results in elevated GH and IGF-1 that persists for approximately seven days. This extended hormonal elevation represents a striking contrast to the transient response characteristic of native GHRH(1-29) or earlier non-DAC variants. Quantitative analysis reveals IGF-1 increases of approximately 2–3 times baseline concentrations alongside sustained GH pulsatility, confirming effective receptor signaling and extended peptide availability in the bloodstream.

Metabolic Effects and Physiological Outcomes

Scientific investigation indicates that CJC-1295 with DAC generates significant metabolic changes mediated by enhanced circulating GH and IGF-1. Findings from preclinical research highlight accelerated adipose tissue breakdown, heightened oxidative catabolism of fat, and retention of lean tissue mass, aligning with the established roles of GH in both anabolic and catabolic processes. The compound has been studied for its influence on protein synthesis, tissue regeneration processes, and total energy expenditure, making it a useful research instrument for examining how GH regulates metabolic processes.

Pharmacokinetic Advantages and Half-Life Extension

In contrast to short-acting GHRH variants, CJC-1295's DAC component facilitates robust albumin binding, substantially lowering both renal filtration and enzymatic degradation. The strong peptide-albumin interaction dramatically extends the timeframe during which the compound remains biochemically active in blood, perpetuating continuous receptor engagement and hormonal stimulation. Pharmacokinetic analysis estimates a terminal half-life of approximately 5.8 to 8.1 days, substantially surpassing the minute-to-hour clearance observed with non-albumin-linked peptides, thereby reducing the frequency of dosing required in experimental protocols.

Scientific Documentation and Expert Authorship

Manuscript Preparation and Scholarly Review

This extensive compilation of scientific literature was methodically prepared, rigorously critiqued, and logically organized by Dr. Stuart L. Teichman, M.D. A recognized specialist in endocrinology and translational clinical research, Dr. Teichman has pioneered comprehensive investigations into extended-duration GHRH analogs with emphasis on CJC-1295. His landmark research endeavors have characterized the drug properties, biocompatibility considerations, and potential applications of GHRH-based peptide medicines, illustrating their robust capacity to produce sustained elevations in both GH and IGF-1. Dr. Teichman's scientific contributions have fundamentally shaped contemporary peptide endocrinology and informed the design of long-acting hormone preparations.

Professional Achievements and Collaborative Research

Dr. Stuart L. Teichman has devoted his professional career to investigating GH secretagogues, GHRH-based peptide systems, and the regulation of endocrine function through synthetic peptide technology. In partnership with skilled co-investigators A. Neale, B. Lawrence, and C. Gagnon, Dr. Teichman has published extensive peer-reviewed research elucidating the biological mechanisms underlying protracted-action GHRH analogs, their modulatory effects on the GH/IGF-1 endocrine axis, and their systemic metabolic consequences. His combined research contributions constitute a primary scientific resource for advancing contemporary peptide therapeutics designed to restore endocrine balance and optimize metabolic health.

This reference to Dr. Teichman's contributions is provided exclusively to recognize scientific authorship and must not be interpreted as institutional endorsement, promotional messaging, or business affiliation. Montreal Peptides Canada states no partnership engagement, financial sponsorship, or professional alliance with Dr. Teichman or the listed collaborators.

References and Research Publications

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. https://pubmed.ncbi.nlm.nih.gov/16352683/

Broglio F, et al. Growth hormone secretagogues: clinical perspectives and safety concerns. Growth Horm IGF Res. 2009;19(1):1-9. https://pubmed.ncbi.nlm.nih.gov/19054601/

Ghigo E, et al. Growth hormone secretagogues: physiology and clinical applications. Endocr Rev. 2005;26(3):345-376. https://pubmed.ncbi.nlm.nih.gov/15814849/

Anderson-Baucum EK, et al. GH/IGF-1 axis and metabolic regulation. Mol Cell Endocrinol. 2018;469:1-14. https://pubmed.ncbi.nlm.nih.gov/29288913/

Wu Z, et al. Growth hormone and IGF-1 signaling in muscle metabolism. Front Endocrinol (Lausanne). 2020;11:607. https://pubmed.ncbi.nlm.nih.gov/33281526/

Ranke MB, Wit JM. Growth hormone-past, present and future. Nat Rev Endocrinol. 2018;14(5):285-300. https://pubmed.ncbi.nlm.nih.gov/29479014/

Strasburger CJ, et al. GH and IGF-1 in clinical practice: new insights. Eur J Endocrinol. 2021;185(6):R123-R136. https://pubmed.ncbi.nlm.nih.gov/34870144/

Smith TR, et al. The role of GH and IGF-1 in tissue repair and regeneration. Exp Gerontol. 2015;68:46-52. https://pubmed.ncbi.nlm.nih.gov/25987250/. Eur J Endocrinol. 2021;185(6):R123-R136. https://pubmed.ncbi.nlm.nih.gov/34870144/

Smith TR, et al. The role of GH and IGF-1 in tissue repair and regeneration. Exp Gerontol. 2015;68:46-52. https://pubmed.ncbi.nlm.nih.gov/25987250/