Investigating the Potential of the Peptide CJC‑1295 (No DAC) in Research Domains
The peptide CJC-1295 (No DAC) is an intriguing synthetic analog of growth-hormone-releasing hormone (GHRH) that continues to attract interest in laboratory research settings. In what follows, we’ll review its molecular properties, receptor interactions, kinetics, and possible research implications — always emphasizing that the discussion remains within the context of research and experimental models.
Molecular and Mechanistic Characteristics
CJC-1295 (No DAC) is often referred to as “Modified GRF (1-29)” because it is believed to trace its lineage to the first 29 amino acids of natural GHRH, with four critical amino-acid substitutions (e.g., D-Ala at position 2, Gln at position 8, Ala at position 15, Leu at position 27) designed to increase resistance to enzymatic degradation.
Unlike the DAC-modified version (which includes a DAC linked to albumin and confers a prolonged half-life), the No DAC version lacks this albumin-binding extension. It therefore displays a comparatively short half-life (on the order of tens of minutes) in controlled experimental conditions.
At the cellular level, the peptide is theorized to bind to the GHRH receptor on anterior-pituitary cells (or equivalent somatotroph-type cells in experimental systems). Studies suggest that upon receptor engagement, a G-protein-coupled cascade may be triggered, generating second messengers such as cyclic AMP or IP₃, activating downstream protein kinases, altering transcription factor activity in the nucleus, and culminating in the release of endogenous growth hormone (GH)-like activity and further signaling (for example via IGF-1 pathways).
Kinetic & Comparative Profile
One of the central distinctions between the No DAC and DAC variants is the half-life and mode of signaling. In one overview, the No DAC variant is described as having a half-life of approximately 30 minutes, whereas the DAC version may persist for 6–10 days under certain conditions.
Because the No DAC version is believed to produce a more acute burst of GH-axis activation, it seems to more closely resemble the natural pulsatile secretion pattern of GHRH/GH in an organism. Some investigators have suggested this makes the No DAC form useful when modeling physiologic GH release, rather than supraphysiologic sustained exposures.
Potential Research Implications
Studies suggest that, given its mechanistic profile, CJC-1295 (No DAC) may have relevance in several distinct research domains. Below are several speculative (but grounded) avenues:
- Modulation of the GH/IGF-1 axis signaling Research
Because the peptide appears to bind to a GHRH receptor analog and trigger GH secretion in a controlled fashion, it may be relevant in experiments designed to examine how transient increases in GH (and consequent IGF-1) support tissue anabolism, metabolism, or repair processes. For example, one might probe how short-burst GH pulses affect downstream gene transcription in muscle-derived models, or how IGF-1-mediated signaling modifies collagen synthesis in fibroblast cultures.
- Tissue-repair and regeneration research
Some sources suggest that analogs of GHRH (including modified GRF forms) may support wound recovery, muscle repair, and possibly bone density through GH/IGF-1-driven pathways. Though direct peer-reviewed data using CJC-1295 (No DAC) are limited, the concept has been theorized in repair- and regeneration-oriented research models.
- Metabolic and lipolytic signaling investigations
Because GH and IGF-1 are implicated in lipid-metabolism regulation, experiments may deploy CJC-1295 (No DAC) as a tool to evaluate lipolysis, adipocyte signaling, or the threshold for lipid-accumulation under conditions of intermittent GH stimulation. Some commentary suggests that GH-axis activation is linked to increased basal metabolic rate and reduced fat deposition. However, this remains speculative in the research specifically for the No DAC variant.
- Sleep-, neuro- and cognitive-function modeling Research
GH secretion is known to be linked with deep-sleep architecture in mammals, and GHRH analogs have been theorized to support sleep quality, slow-wave sleep, and, consequently, cognitive processes. Although direct experimental work with CJC-1295 (No DAC) in this domain appears limited, the peptide is hypothesized to be utilized in research models investigating how bursts of GH-axis activation support sleep-related gene expression, neurotrophic factors, or brain-derived growth factor (BDNF) pathways.
- Endocrine-feedback and receptor-sensitivity research
Because the No DAC version seems to offer a relatively short-acting stimulus, it may be valuable for researchers investigating feedback loops within the GH/IGF-1 system: for example, how short bursts of GH support somatostatin release, GH-receptor sensitivity, IGF-binding protein modulation, or downstream receptor down-regulation. Because the DAC variant appears to produce sustained activation, using the No DAC form may help preserve more physiologic fluctuation and avoid artifacts introduced by persistent exposure.
Concluding Remarks
In summary, the peptide CJC-1295 (No DAC) emerges as a versatile research tool for investigators interested in modeling the GH/IGF-1 axis, exploring pulsatile endocrine signaling, and probing downstream cellular and tissue responses to short-acting GHRH analogs. Its design – lacking the DAC complex and thus featuring a relatively brief half-life – makes it particularly suited for experiments that aim to mimic physiologic bursts of GH-axis activity rather than prolonged exposure.
While peer-reviewed data specific to the No DAC variant remain modest compared to its DAC counterpart, the mechanistic rationale and preliminary characterization support its use in multiple research domains: from tissue repair and metabolic modulation to neuro-endocrine and sleep-linked signaling. Future work that further delineates its kinetics, receptor-dynamics, tissue-responses, and combination-synergies will deepen our understanding of GH-axis manipulation in the laboratory. Visit https://www.corepeptides.com/peptides/cjc-1295-no-dac-mod-grf-1-29/ for the best research materials available online.
References
[i] Schally, A. V., Lobel, P., & Cai, R. Z. (2018). Growth hormone-releasing hormone (GHRH) and its agonists inhibit hepatic and tumoral secretion of IGF-1. Oncotarget, 9(47), 28 745-28 756. https://doi.org/10.18632/oncotarget.25676
[ii] Douglass, L. M., & Frohman, L. A. (1999). Growth Hormone (GH)-Releasing Hormone (GHRH) and the GH secretagogue (GHS), L692,585, differentially modulate rat pituitary GHS receptor and GHRH receptor messenger ribonucleic acid levels. Endocrinology, 140(8), 3581-3586. https://doi.org/10.1210/endo.140.8.3581
[iii] Okada, R., et al. (2006). Bioactivity of growth hormone-releasing hormone (1-29) analogs after SC injection in man. Journal of Endocrinological Investigation, 29(6), 503-507. https://doi.org/10.1007/BF03345382
[iv] Cai, R.-Z., et al. (2005). Human growth hormone-releasing factor (hGRF)1–29-albumin bioconjugates activate the GRF receptor on the anterior pituitary in rats: Identification of CJC-1295 as a long-lasting GRF analog. Endocrinology, 146(7), 3052-3058. https://doi.org/10.1210/en.2004-1207
[v] Yang, J., et al. (2023). Growth hormone-releasing hormone receptor (GHRH-R) and its signaling. Neural Regeneration Research, 18(12), 2609-2618. https://doi.org/10.4103/1673-5374.374339
