Peptide Insider Editorial Research Desk · 2026-09-25 · Mechanism & Pathways · Research reference only
Search logs for the growth-hormone-releasing-hormone (GHRH) analogue family are dominated by a single lexical fork: cjc-1295 without dac versus cjc-1295 w/dac, with the question what does no dac mean in peptides appearing alongside dual listings such as cjc-no dac / ipamorelin and tesamorelin & ipamorelin blend. Behind that fork sits one of the clearest structure-to-pharmacokinetics stories in peptide chemistry: a 29-residue fragment of a 44-residue hypothalamic hormone, a dipeptidyl-peptidase cleavage site that limits its plasma survival to minutes, four amino-acid substitutions that close that site, and a maleimide linker that covalently parks the peptide on serum albumin. This review traces that lineage from sermorelin to Mod GRF 1-29, CJC-1295 and tesamorelin, records the selective ghrelin-receptor agonist ipamorelin that is routinely co-listed with them, and then classifies the catalogue vocabulary into research-scope terms and out-of-scope (dosage, therapeutic, price) terms.
Direct answer. “DAC” stands for Drug Affinity Complex: a maleimidopropionic-acid (MPA) group attached through a C-terminal lysine (Lys30) that forms a covalent thioether bond with the free Cys34 thiol of circulating albumin [10] [15] [16]. “No DAC” (Mod GRF 1-29) is the identical tetrasubstituted GRF(1-29)NH2 peptide (D-Ala2, Gln8, Ala15, Leu27) without that linker. In the published human pharmacokinetic study, the albumin-bound form exhibited an elimination half-life of roughly 5.8–8.1 days, whereas unmodified GRF(1-29) is degraded in plasma within minutes [11] [5]. Sermorelin is native GRF(1-29)NH2; tesamorelin is the full 44-residue GHRH carrying an N-terminal trans-3-hexenoyl group. All four are GHRH-receptor (GHRHR) agonists; ipamorelin is a pentapeptide agonist of a different receptor, GHS-R1a [21].
1. The parent sequence: from GHRH(1-44) to GRF(1-29)
Human GHRH was isolated in 1982 from pancreatic islet tumours associated with acromegaly, and characterised as a 44-residue amidated peptide (with 40- and 37-residue forms also present) [1] [2]. Structure–activity studies established that the N-terminal 29 residues carry essentially all receptor-binding and GH-releasing activity: analogues and fragments were compared for pituitary receptor binding and cAMP/GH release, and truncation beyond residue 29 sharply reduced potency while residues 30–44 were dispensable [3]. Systematic analogue series confirmed that residues Tyr1, Ala2, Asp3, and the amphipathic helix spanning roughly residues 6–27 are the principal pharmacophores, with Lys12, Lys21, Leu22 and Leu23 contributing to receptor affinity [4].
That 29-residue amide, GRF(1-29)NH2, is sermorelin (International Nonproprietary Name; the “-relin” stem denotes a releasing-factor analogue, pronounced ser-mo-REL-in). It was formulated as the acetate salt and reviewed as a diagnostic and paediatric agent in the 1990s [8]; a later commentary discussed it in the context of adult somatotropic insufficiency [9]. In research catalogues it appears as sermorelin research peptide or sermorelin powder, and in misspelled forms such as sermorelon and semorellin. The receptor it targets, GHRHR, is a class B G-protein-coupled receptor cloned from rat and human pituitary in 1992–1993; it signals through Gαs and adenylyl cyclase to raise somatotroph cAMP [24] [25].
2. Why GRF(1-29) is short-lived: the Ala2–Asp3 cleavage site
Frohman and colleagues showed in 1986 that GHRH incubated in human plasma is rapidly converted to a biologically inactive product cleaved at the NH2 terminus, and that the same conversion occurs in vivo [5]. The follow-up study identified the responsible enzyme as dipeptidyl peptidase IV (DPP-IV, CD26), which removes the N-terminal Tyr1-Ala2 dipeptide to yield GHRH(3-44), with a secondary trypsin-like cleavage contributing at basic residues [6]. Parallel work on rat GRF(1-29)NH2 in serum and liver confirmed rapid N-terminal and internal proteolysis [7]. Because Tyr1 and Ala2 are pharmacophores, the DPP-IV product has negligible activity; the plasma half-life of native GRF(1-29) in the human study was on the order of minutes [11].
This is the mechanistic reason every longer-acting analogue in the family modifies the N-terminus. Two design routes appear in the literature: (a) substitute residue 2 with a D-amino acid so DPP-IV cannot recognise the Xaa-Ala/Pro motif, and (b) cap the N-terminus with an acyl group. Route (a) produced Mod GRF 1-29 and CJC-1295; route (b) produced tesamorelin.
3. Mod GRF 1-29 (“CJC-1295 without DAC”): the four substitutions
The peptide core of CJC-1295 is GRF(1-29)NH2 carrying four substitutions: D-Ala2, Gln8, Ala15 and Leu27 [10]. Each has a stability rationale. D-Ala2 blocks DPP-IV cleavage. Gln8 replaces Asn8, removing a deamidation-prone asparagine (Asn-Ser and Asn-Gly motifs deamidate via succinimide intermediates under storage) [27]. Ala15 replaces Gly15, increasing helix propensity and reported receptor affinity in analogue series [3] [4]. Leu27 replaces Met27, removing the sulfur-containing residue most susceptible to oxidation [27]. This tetrasubstituted peptide is what catalogues call cjc-1295 without dac, cjc-1295 w/o dac, cjc no dac peptide or Mod GRF 1-29; the query cjc-1295 no dac amino acid substitutions resolves to exactly this list. Strictly, the developer’s designation CJC-1295 refers to the albumin-binding conjugate, so “CJC-1295 without DAC” is a catalogue back-formation rather than a literature name [10].
4. The Drug Affinity Complex: covalent albumin binding at Cys34
Human serum albumin (UniProt P02768) carries 35 cysteines, 34 of which are disulfide-paired; Cys34 is the single free thiol and is the most reactive nucleophile in plasma. Maleimide groups react with it selectively to form a stable thioether, a strategy reviewed extensively as an approach to half-life extension because albumin itself circulates for about 19 days through FcRn-mediated recycling [15] [16]. Jetté and colleagues appended a maleimidopropionic-acid (MPA) group to an added Lys30 on the tetrasubstituted GRF(1-29) core; the resulting compound (CJC-1295) formed bioconjugates with rat and human albumin in vitro and, after administration in rats, remained detectable as an albumin conjugate that continued to activate the pituitary GRF receptor and elevate GH and IGF-1 for days rather than minutes [10].
The human pharmacology was reported by Teichman et al. in a randomised, placebo-controlled study of healthy adults: single administrations of CJC-1295 produced dose-dependent increases in mean plasma GH (approximately 2- to 10-fold) for six days or more and in IGF-1 (approximately 1.5- to 3-fold) for nine to eleven days, with an estimated elimination half-life of 5.8–8.1 days; after multiple administrations, IGF-1 remained elevated for up to 28 days [11]. Ionescu and Frohman then showed that the physiological pulsatility of GH secretion was preserved during continuous GHRHR stimulation by CJC-1295, with pulse amplitude rather than pulse frequency increased [12]. In GHRH-knockout mice, once-daily CJC-1295 restored body-weight gain and normalised pituitary GH content [13], and serum proteomic profiling in adult subjects documented the downstream protein-level footprint of GH/IGF-1 axis activation [14]. In catalogue orthography this compound is cjc-1295 w/dac, cjc-1295 w dac, cjc 1295 dac peptide, cjc1295dac or cjc dac 1295; the questions what is dac in cjc 1295, what is cjc 1295 dac and cjc and dac all resolve to the MPA–albumin chemistry described here.
5. Tesamorelin: N-terminal acylation of the full 44-residue sequence
Tesamorelin (TH9507; DrugBank DB06285) takes the alternative design route: it is the complete human GHRH(1-44)NH2 sequence with a trans-3-hexenoyl group on the N-terminal tyrosine. Non-clinical pharmacology showed the acyl cap conferred resistance to DPP-IV cleavage and a longer functional duration than native GHRH while retaining full GHRHR agonism and native-like GH pulsatility [17]. Its clinical literature is unusually large for this family: a phase 3 randomised trial published in the New England Journal of Medicine in 2007 [18], a pooled analysis of two phase 3 trials in 2010 [19], and a 2014 randomised trial in JAMA measuring visceral and hepatic fat by imaging [20]. Those reports describe the compound’s effects in a specific patient population under medical supervision; they are cited here as literature record and for mechanistic comparison only, not as guidance for any use of research-grade material. The catalogue tokens ipamorelin tesamorelin, tesa ipamorelin, tesamorelin & ipamorelin blend, tesamorelin + ipamorelin blend and tesamorelin cjc1295 ipamorelin pair it with GHS-R agonists, as discussed next.
6. Ipamorelin: why the second receptor is co-listed
GH release from the somatotroph is governed by two stimulatory receptors and one inhibitory input: GHRHR (agonised by all four analogues above), the growth hormone secretagogue receptor GHS-R1a (UniProt Q92847; the ghrelin receptor), and somatostatin receptors. Muller, Locatelli and Cocchi’s comprehensive Physiological Reviews article describes how GHRHR and GHS-R agonists act on distinct second-messenger systems (cAMP versus phospholipase C/Ca2+) and interact synergistically at the somatotroph and hypothalamus [23]. Bowers’ review of the growth hormone-releasing peptides traces the GHRP lineage from met-enkephalin-derived hexapeptides to the identification of GHS-R [22]. Ipamorelin (Aib-His-D-2-Nal-D-Phe-Lys-NH2) was characterised by Raun et al. in 1998 as the first GHS with selectivity for GH release over ACTH and cortisol in rat and swine models, with in-vivo potency similar to GHRP-6 [21]. A 2020 narrative review in Translational Andrology and Urology summarises the secretagogue class, including the CJC-1295/ipamorelin pairing, from a clinical-literature standpoint [26]. This dual-receptor logic is why catalogue listings such as cjc 1295 no dac / ipamorelin, cjc 1295 no dac + ipamorelin, ipamorelin / cjc-1295 no dac, ipamorelin cjc-1295 without dac, cjc ipamorelin no dac, cjc 1295 dac ipamorelin, cjc-1295 & ipamorelin blend, ipamorelin + cjc-1295, cjc-1295/ipamorelin peptides, cjc-1295/ipamorelin peptide, peptides cjc 1295 ipamorelin, ipa/cjc-1295, cjc1295 no dac ipamorelin and the misspelling cj1295 ipamorelin exist: they name a GHRHR agonist and a GHS-R1a agonist in one line. Triple listings (sermorelin ipamorelin and cjc 1295, sermorelin ipamorelin cjc 1295, tesamorelin & mod grf & ipamorelin blend) combine two GHRHR agonists with one GHS-R agonist and have no dedicated literature.
7. Evidence table
| Compound / modification | Research model | Signal vector | Key observation | Ref |
|---|---|---|---|---|
| GHRH(1-44)NH2, native | Human pancreatic islet tumour isolation; rat pituitary bioassay | GH release, sequence | 44-residue amide identified; 40/37-residue forms co-isolated | [1] [2] |
| GRF(1-29)NH2 (sermorelin) | Rat pituitary membranes; analogue/fragment series | Receptor binding, cAMP, GH | Residues 1-29 retain full activity; C-terminal 30-44 dispensable | [3] [4] |
| GHRH in plasma | Human plasma in vitro; human in vivo | HPLC/RIA of fragments | DPP-IV cleaves Tyr1-Ala2 within minutes; product inactive | [5] [6] |
| rGRF(1-29)NH2 | Rat serum and liver | HPLC catabolite mapping | N-terminal and internal proteolysis | [7] |
| Mod GRF 1-29 core (D-Ala2, Gln8, Ala15, Leu27) | Design rationale; rat pituitary cells | cAMP, GH | Substitutions confer DPP-IV resistance and chemical stability | [10] [27] |
| CJC-1295 (Lys30-MPA conjugate) | Rat in vivo; albumin bioconjugation in vitro | Albumin-conjugate detection; GH, IGF-1 | Covalent albumin binding; multi-day GH/IGF-1 elevation | [10] |
| CJC-1295 | Healthy adults, randomised placebo-controlled | Plasma GH, IGF-1, PK | t1/2 5.8-8.1 d; IGF-1 elevated 9-11 d after single administration | [11] |
| CJC-1295 | Healthy adults, frequent sampling | GH pulse analysis | Pulsatility preserved; amplitude increased | [12] |
| CJC-1295 | GHRH-knockout mouse | Body weight, pituitary GH | Once-daily administration normalised growth | [13] |
| CJC-1295 | Adult subjects, serum proteomics | 2-D gel protein profile | GH/IGF-1-dependent serum protein changes | [14] |
| Albumin Cys34 maleimide chemistry | Review | Half-life extension platform | FcRn recycling gives ~19 d albumin half-life | [15] [16] |
| Tesamorelin (trans-3-hexenoyl-GHRH(1-44)) | Non-clinical pharmacology/toxicology | GH, IGF-1; stability | DPP-IV resistance with native-like pulsatility | [17] |
| Tesamorelin | Phase 3 RCTs and pooled analysis (patient population) | CT-measured adipose depots, IGF-1 | Clinical literature record; outside RUO scope | [18] [19] [20] |
| Ipamorelin (Aib-His-D-2-Nal-D-Phe-Lys-NH2) | Rat pituitary cells; rat and swine in vivo | GH, ACTH, cortisol | GH-selective GHS; no ACTH/cortisol rise | [21] |
| GHRHR / GHS-R axis | Reviews; receptor cloning | cAMP vs PLC/Ca2+ | Distinct receptors; synergistic somatotroph activation | [22] [23] [24] [25] |
8. Catalogue-vocabulary crosswalk and RUO scope status
The following table records verbatim query strings observed in research-catalogue search logs, maps each to its chemical referent, and states its research-use-only scope status. Strings classified as Declined carry dosage, therapeutic, tolerability, consumer dosage-form or price semantics and receive no substantive answer on this site; they are listed solely so the reader can see how the nomenclature is used and why those framings fall outside a research review. Note the fill-mass strings (for example ipamorelin 10 mg) describe lyophilised net peptide per vial and are not administration quantities.
| Verbatim query string | Chemical referent / classification | RUO scope status |
|---|---|---|
| cjc-1295 without dac | Mod GRF 1-29 (tetrasubstituted GRF(1-29)NH2 without the MPA linker) | Recorded as nomenclature |
| cjc-1295 w/dac | CJC-1295 proper: Mod GRF 1-29 + Lys30-MPA Drug Affinity Complex | Recorded as nomenclature |
| cjc-1295 w dac | Same as above; whitespace variant | Recorded as nomenclature |
| cjc-1295 w/o dac | Mod GRF 1-29; abbreviation variant | Recorded as nomenclature |
| cjc-1295 no-dac | Mod GRF 1-29; hyphen variant | Recorded as nomenclature |
| cjc-no dac | Mod GRF 1-29; truncated variant | Recorded as nomenclature |
| cjc no dac peptide | Mod GRF 1-29 | Recorded as nomenclature |
| no dac peptide | Any GRF(1-29) analogue lacking the albumin-binding linker | Recorded as terminology |
| what does no dac mean in peptides | Absence of the maleimidopropionic-acid albumin-binding linker | Recorded as terminology (question form) |
| what is dac in cjc 1295 | Drug Affinity Complex: Lys30-MPA that binds albumin Cys34 | Recorded as terminology (question form) |
| what is cjc 1295 dac | CJC-1295 with the albumin-binding linker | Recorded as nomenclature (question form) |
| what is cjc-1295 with dac | Same referent | Recorded as nomenclature (question form) |
| what is cjc 1295 no dac | Mod GRF 1-29 | Recorded as nomenclature (question form) |
| what is cjc 1295 peptide | Family-level query; either variant | Recorded as nomenclature (question form) |
| cjc-1295 peptide what is it | Family-level query | Recorded as nomenclature (question form) |
| cjc-1295 no dac amino acid substitutions | D-Ala2, Gln8, Ala15, Leu27 | Recorded as terminology |
| cjc 1295 dac peptide | CJC-1295 with DAC | Recorded as nomenclature |
| cjc-1295 dac peptide | CJC-1295 with DAC; hyphen variant | Recorded as nomenclature |
| cjc 1295 with dac peptide | CJC-1295 with DAC | Recorded as nomenclature |
| cjc dac 1295 | Token re-ordering | Recorded as nomenclature |
| cjc and dac | Family + linker tokens | Recorded as nomenclature |
| cjc1295dac | Whitespace collapse | Recorded as orthographic variant |
| cjc1295 no dac ipamorelin | Mod GRF 1-29 + ipamorelin dual-agonist listing | Recorded as nomenclature |
| cj1295 ipamorelin | Digit-drop misspelling of CJC-1295 + ipamorelin | Recorded as orthographic variant |
| peptide cjc1295 | Whitespace collapse | Recorded as orthographic variant |
| cjc 5 | Prefix truncation (ambiguous) | Recorded as orthographic variant |
| cjc-no dac / ipamorelin | Dual-agonist listing (GHRH-R + GHS-R) | Recorded as nomenclature |
| cjc 1295 no dac / ipamorelin | Dual-agonist listing | Recorded as nomenclature |
| cjc 1295 no dac + ipamorelin | Dual-agonist listing | Recorded as nomenclature |
| ipamorelin / cjc-1295 no dac | Dual-agonist listing, reversed order | Recorded as nomenclature |
| ipamorelin cjc-1295 without dac | Dual-agonist listing | Recorded as nomenclature |
| cjc ipamorelin no dac | Dual-agonist listing | Recorded as nomenclature |
| cjc 1295 dac ipamorelin | CJC-1295 with DAC + ipamorelin listing | Recorded as nomenclature |
| cjc-1295 & ipamorelin blend | Dual-agonist listing (linker unspecified) | Recorded as nomenclature |
| ipamorelin + cjc-1295 | Dual-agonist listing | Recorded as nomenclature |
| cjc-1295/ipamorelin peptides | Dual-agonist listing | Recorded as nomenclature |
| cjc-1295/ipamorelin peptide | Dual-agonist listing | Recorded as nomenclature |
| peptides cjc 1295 ipamorelin | Dual-agonist listing | Recorded as nomenclature |
| ipa/cjc-1295 | Abbreviated dual-agonist listing (IPA = ipamorelin) | Recorded as nomenclature |
| cjc 1295 ipamorelin half life | Pharmacokinetic query; see Table 1 (Teichman 2006; Raun 1998) | Recorded as terminology (question form) |
| sermorelin ipamorelin and cjc 1295 | Triple listing across GHRH-R and GHS-R agonists | Recorded as nomenclature |
| sermorelin ipamorelin cjc 1295 | Triple listing | Recorded as nomenclature |
| tesamorelin cjc1295 ipamorelin | Triple listing | Recorded as nomenclature |
| tesamorelin & mod grf & ipamorelin blend | Triple listing naming Mod GRF 1-29 explicitly | Recorded as nomenclature |
| sermorelon | Vowel substitution misspelling of sermorelin | Recorded as orthographic variant |
| semorellin | Consonant drop/double misspelling of sermorelin | Recorded as orthographic variant |
| sermorelin. | Trailing punctuation variant | Recorded as orthographic variant |
| sermorelin research peptide | GRF(1-29)NH2 acetate | Recorded as nomenclature |
| sermorelin powder | Lyophilised presentation descriptor | Recorded as catalogue terminology |
| how to pronounce sermorelin | ser-mo-REL-in (INN stem -relin = releasing-factor analogue) | Recorded as terminology (question form) |
| sermorelin pronounce | Same referent | Recorded as terminology |
| sermorelin peptide what does it do | GHRH-R agonist; see Mechanism section | Recorded as terminology (question form) |
| what does ipamorelin peptide do | GHS-R1a agonist; see Mechanism section | Recorded as terminology (question form) |
| ipamorelin tesamorelin | Dual-agonist listing (GHRH-R + GHS-R) | Recorded as nomenclature |
| tesa ipamorelin | Abbreviated dual listing (tesa = tesamorelin) | Recorded as nomenclature |
| tesamorelin & ipamorelin blend | Dual-agonist listing | Recorded as nomenclature |
| tesamorelin + ipamorelin blend | Dual-agonist listing | Recorded as nomenclature |
| ipamorelin 10 mg | Catalogue fill-mass descriptor (lyophilised net peptide) | Recorded as catalogue terminology |
| ipamorelin 2mg | Catalogue fill-mass descriptor | Recorded as catalogue terminology |
| cjc-1295 dac 10mg | Catalogue fill-mass descriptor | Recorded as catalogue terminology |
| tesamorelin peptide 10 mg | Catalogue fill-mass descriptor | Recorded as catalogue terminology |
| tesamorelin/ipamorelin dosage | Dosage query | Declined - dosage |
| tesamorelin + ipamorelin blend dosage per day | Dosage query | Declined - dosage |
| sermorelin peptide dosage chart | Dosage query | Declined - dosage |
| cjc-1295 with dac dosing protocol | Dosage/protocol query | Declined - dosage |
| tesamorelin cjc1295 ipamorelin 12mg blend dose | Dosage query | Declined - dosage |
| how much bacteriostatic water to mix with 5mg of cjc-1295 | Preparation-protocol query | Declined - protocol |
| sermorelin hair growth | Outcome/benefit claim | Declined - health claim |
| cjc 1295 with dac benefits | Outcome/benefit claim | Declined - health claim |
| cjc-1295 + ipamorelin muscle growth | Outcome/benefit claim | Declined - health claim |
| cjc-1295 ipamorelin body recomposition | Outcome/benefit claim | Declined - health claim |
| cjc 1295 ipamorelin peptide therapy | Therapeutic-use framing | Declined - human use |
| side effects of cjc 1295 dac | Human tolerability query | Declined - human use |
| cjc 1295 ipamorelin hot flush | Human tolerability query | Declined - human use |
| sermorelin peptide supplement | Supplement framing | Declined - human use |
| sermorelin otc | Over-the-counter framing | Declined - human use |
| sermorelin mints | Consumer dosage-form framing | Declined - human use |
| tesamorelin tablets for sale | Consumer dosage-form + commerce | Declined - promo |
| compounded tesamorelin | Pharmacy-compounding framing | Declined - human use |
| how much does tesamorelin cost | Price query | Declined - promo/price |
| tesamorelin prices | Price query | Declined - promo/price |
| why is tesamorelin so expensive | Price query | Declined - promo/price |
9. Handling notes for the lyophilised analogues
All four GHRHR agonists and ipamorelin are supplied to laboratories as lyophilised powders. The stability considerations reviewed by Manning et al. apply directly: the native Asn8 and Met27 of sermorelin are deamidation- and oxidation-prone, which is precisely why Mod GRF 1-29 substitutes them; tesamorelin retains Asn8 and Met27 and the additional Met and Asn residues of the 30-44 tail; and the maleimide of CJC-1295 is itself a reactive electrophile that will hydrolyse or react with thiol-containing excipients in solution, so the conjugate is only meaningful when formed in the presence of albumin [27]. Certificates of analysis should therefore report RP-HPLC purity and mass-spectrometric identity for the intact sequence, and for CJC-1295 confirm that the MPA group is present. Reconstitution-solvent chemistry is covered in our reconstitution-solvent review; the individual compound reviews for CJC-1295, tesamorelin and ipamorelin, the somatotropic-axis nomenclature review, the MK-677 non-peptide secretagogue review and the receptor-family index provide the wider context.
10. Frequently asked research questions
What does no dac mean in peptides?
“No DAC” means the GRF(1-29) analogue lacks the Drug Affinity Complex: the maleimidopropionic-acid group on Lys30 that covalently binds albumin Cys34. The peptide is otherwise identical to the CJC-1295 core (D-Ala2, Gln8, Ala15, Leu27) and is properly called Mod GRF 1-29 [10].
What is cjc 1295 dac and how does it differ from sermorelin?
CJC-1295 with DAC is a tetrasubstituted GRF(1-29)NH2 carrying an albumin-binding linker; sermorelin is the unmodified native GRF(1-29)NH2. In plasma the native peptide is cleaved by DPP-IV within minutes, whereas the albumin-bound conjugate showed an elimination half-life of 5.8–8.1 days in the published human study [5] [6] [11].
What are the cjc-1295 no dac amino acid substitutions?
D-Ala2 (blocks DPP-IV), Gln8 (removes a deamidation-prone Asn), Ala15 (increases helicity and affinity) and Leu27 (removes an oxidation-prone Met), relative to native GRF(1-29) [10] [27].
What is the cjc 1295 ipamorelin half life relationship?
They are separate molecules with separate kinetics. Albumin-bound CJC-1295 has a multi-day half-life [11]; ipamorelin, a pentapeptide without a half-life-extension moiety, showed a short duration of GH release in the original rat and swine characterisation [21]. Co-listing does not create a shared half-life.
What does ipamorelin peptide do at the receptor level, and why is it paired with GHRH analogues?
Ipamorelin is a GHS-R1a agonist that stimulates GH release without raising ACTH or cortisol in the rat and swine models studied [21]. GHS-R1a and GHRHR use different second-messenger systems and act synergistically at the somatotroph, which is the mechanistic basis for dual listings such as cjc-no dac / ipamorelin [23].
Is tesamorelin/ipamorelin dosage or sermorelin peptide dosage chart information provided here?
No. Strings such as tesamorelin/ipamorelin dosage, sermorelin peptide dosage chart and cjc-1295 with dac dosing protocol are recorded in the crosswalk as Declined. The compounds discussed are research reagents; this review reports mechanism and published literature only and gives no administration guidance.
11. Where to source for research
Research-grade sermorelin, Mod GRF 1-29, CJC-1295 (DAC), tesamorelin and ipamorelin are catalogued by several research-reagent suppliers, including Short Chain Aminos, BioPep, Catalyst Research and Apex Research Services. This is a statement of research availability only; no vendor has been assessed or endorsed. Researchers should request lot-specific certificates of analysis confirming sequence identity by mass spectrometry, RP-HPLC purity and, for CJC-1295, presence of the MPA linker, and should confirm that any material is labelled for laboratory research use.
Works Cited
- Rivier J, Spiess J, Thorner M, Vale W. Characterization of a growth hormone-releasing factor from a human pancreatic islet tumour. Nature. 1982;300:276-278. PMID: 6292724. DOI: 10.1038/300276a0.
- Guillemin R, Brazeau P, Bohlen P, et al. Growth hormone-releasing factor from a human pancreatic tumor that caused acromegaly / characterization of a 40-residue peptide. Biochem Biophys Res Commun. 1982. PMID: 7159418. DOI: 10.1016/0006-291x(82)91578-9.
- Campbell RM, Lee Y, Rivier J, et al. GRF analogs and fragments: correlation between receptor binding, activity and structure. Peptides. 1991;12(3):569-574. PMID: 1656403. DOI: 10.1016/0196-9781(91)90103-v.
- Gaudreau P, Boulanger L, Abribat T. Affinity of human growth hormone-releasing factor (1-29)NH2 analogues for GRF binding sites in rat adenopituitary. J Med Chem. 1992;35(10):1864-1869. PMID: 1534126. DOI: 10.1021/jm00088a023.
- Frohman LA, Downs TR, Williams TC, et al. Rapid enzymatic degradation of growth hormone-releasing hormone by plasma in vitro and in vivo to a biologically inactive product cleaved at the NH2 terminus. J Clin Invest. 1986;78(4):906-913. PMID: 3093533. DOI: 10.1172/JCI112679.
- Frohman LA, Downs TR, Heimer EP, Felix AM. Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma. J Clin Invest. 1989;83(5):1533-1540. PMID: 2565342. DOI: 10.1172/JCI114049.
- Boulanger L, Roughly P, Gaudreau P. Catabolism of rat growth hormone-releasing factor(1-29) amide in rat serum and liver. Peptides. 1992;13(4):681-689. PMID: 1437711. DOI: 10.1016/0196-9781(92)90173-z.
- Prakash A, Goa KL. Sermorelin: a review of its use in the diagnosis and treatment of children with idiopathic growth hormone deficiency. BioDrugs. 1999;12(2):139-157. PMID: 18031173. DOI: 10.2165/00063030-199912020-00007.
- Walker RF. Sermorelin: a better approach to management of adult-onset growth hormone insufficiency? Clin Interv Aging. 2006;1(4):307-308. PMID: 18046908. DOI: 10.2147/ciia.2006.1.4.307.
- Jette L, Leger R, Thibaudeau K, et al. 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. 2005;146(7):3052-3058. PMID: 15817669. DOI: 10.1210/en.2004-1286.
- Teichman SL, Neale A, Lawrence B, et al. Prolonged stimulation of growth hormone (GH) and insulin-like growth factor I secretion by CJC-1295, a long-acting analog of GH-releasing hormone, in healthy adults. J Clin Endocrinol Metab. 2006;91(3):799-805. PMID: 16352683. DOI: 10.1210/jc.2005-1536.
- Ionescu M, Frohman LA. Pulsatile secretion of growth hormone (GH) persists during continuous stimulation by CJC-1295, a long-acting GH-releasing hormone analog. J Clin Endocrinol Metab. 2006;91(12):4792-4797. PMID: 17018654. DOI: 10.1210/jc.2006-1702.
- Alba M, Fintini D, Sagazio A, et al. Once-daily administration of CJC-1295, a long-acting growth hormone-releasing hormone (GHRH) analog, normalizes growth in the GHRH knockout mouse. Am J Physiol Endocrinol Metab. 2006;291(6):E1290-E1294. PMID: 16822960. DOI: 10.1152/ajpendo.00201.2006.
- Sackmann-Sala L, Ding J, Frohman LA, Kopchick JJ. Activation of the GH/IGF-1 axis by CJC-1295, a long-acting GHRH analog, results in serum protein profile changes in normal adult subjects. Growth Horm IGF Res. 2009;19(6):471-477. PMID: 19386527. DOI: 10.1016/j.ghir.2009.03.001.
- Kratz F. Albumin as a drug carrier: design of prodrugs, drug conjugates and nanoparticles. J Control Release. 2008;132(3):171-183. PMID: 18582981. DOI: 10.1016/j.jconrel.2008.05.010.
- Sleep D, Cameron J, Evans LR. Albumin as a versatile platform for drug half-life extension. Biochim Biophys Acta. 2013;1830(12):5526-5534. PMID: 23639804. DOI: 10.1016/j.bbagen.2013.04.023.
- Ferdinandi ES, Brazeau P, High K, et al. Non-clinical pharmacology and safety evaluation of TH9507, a human growth hormone-releasing factor analogue. Basic Clin Pharmacol Toxicol. 2007;100(1):49-58. PMID: 17214611. DOI: 10.1111/j.1742-7843.2007.00008.x.
- Falutz J, Allas S, Blot K, et al. Metabolic effects of a growth hormone-releasing factor in patients with HIV. N Engl J Med. 2007;357(23):2359-2370. PMID: 18057338. DOI: 10.1056/NEJMoa072375.
- Falutz J, Mamputu JC, Potvin D, et al. Effects of tesamorelin (TH9507), a growth hormone-releasing factor analog, in HIV-infected patients with excess abdominal fat: a pooled analysis of two multicenter, double-blind placebo-controlled phase 3 trials. J Clin Endocrinol Metab. 2010;95(9):4291-4304. PMID: 20554713. DOI: 10.1210/jc.2010-0490.
- Stanley TL, Feldpausch MN, Oh J, et al. Effect of tesamorelin on visceral fat and liver fat in HIV-infected patients with abdominal fat accumulation: a randomized clinical trial. JAMA. 2014;312(4):380-389. PMID: 25038357. DOI: 10.1001/jama.2014.8334.
- Raun K, Hansen BS, Johansen NL, et al. Ipamorelin, the first selective growth hormone secretagogue. Eur J Endocrinol. 1998;139(5):552-561. PMID: 9849822. DOI: 10.1530/eje.0.1390552.
- Bowers CY. Growth hormone-releasing peptide (GHRP). Cell Mol Life Sci. 1998;54(12):1316-1329. PMID: 9893708. DOI: 10.1007/s000180050257.
- Muller EE, Locatelli V, Cocchi D. Neuroendocrine control of growth hormone secretion. Physiol Rev. 1999;79(2):511-607. PMID: 10221989. DOI: 10.1152/physrev.1999.79.2.511.
- Mayo KE. Molecular cloning and expression of a pituitary-specific receptor for growth hormone-releasing hormone. Mol Endocrinol. 1992;6(10):1734-1744. PMID: 1333056. DOI: 10.1210/mend.6.10.1333056.
- Gaylinn BD, Harrison JK, Zysk JR, et al. Molecular cloning and expression of a human anterior pituitary receptor for growth hormone-releasing hormone. Mol Endocrinol. 1993;7(1):77-84. PMID: 7680413. DOI: 10.1210/mend.7.1.7680413.
- Sinha DK, Balasubramanian A, Tatem AJ, et al. Beyond the androgen receptor: the role of growth hormone secretagogues in the modern management of body composition in hypogonadal males. Transl Androl Urol. 2020;9(Suppl 2):S149-S159. PMID: 32257855. DOI: 10.21037/tau.2019.11.30.
- Manning MC, Chou DK, Murphy BM, et al. Stability of protein pharmaceuticals: an update. Pharm Res. 2010;27(4):544-575. PMID: 20143256. DOI: 10.1007/s11095-009-0045-6.
Research Use Only Disclaimer. This article is an academic literature review of peptide chemistry and pharmacology. The compounds described are strictly for research reference; not for human or veterinary use. No dosing, administration, therapeutic, diagnostic or health information is provided or implied, and the clinical trials cited are summarised solely as published literature.