CJC-1295 with DAC

CJC-1295 with DAC in brief

CJC-1295 with DAC is a 30-residue analogue of the first 29 residues of human growth hormone-releasing hormone, carrying D-alanine at 2, glutamine at 8, alanine at 15 and leucine at 27, plus an added C-terminal lysine whose side chain bears a maleimide (C165H269N47O46, about 3647.2 g/mol). Each substitution answers a chemical liability of the parent fragment. The maleimide reacts with a free protein thiol, principally albumin cysteine 34, so what circulates is a protein conjugate. The name is ambiguous in the published record, often used for the 29-residue peptide with no maleimide. No receptor affinity or potency figure for this molecule was found, and no structure exists.^[1,2,3,4,5]

CJC-1295 with DAC regulatory status

CJC-1295 with DAC holds no marketing authorisation: Drugs@FDA, the European Medicines Agency medicines database and the Health Canada Drug Product Database return no record of it (all searched November 2026), and the one registered trial found on ClinicalTrials.gov under the name, a phase 2 study in HIV-associated visceral adiposity sponsored by ConjuChem, is recorded as terminated. CJC-1295 is named on the World Anti-Doping Agency 2026 Prohibited List under S2.2.4 as a growth hormone-releasing hormone analogue, a non-specified substance prohibited at all times. The FDA's list of bulk drug substances that may present significant safety risks (current as of 22 April 2026) places a substance named CJC-1295, without specifying either form, among substances previously in category 2 whose nominations were withdrawn by the nominators, stating a possible risk of immunogenicity and complexities with peptide-related impurities and characterisation of the active ingredient, that the FDA has identified serious adverse events associated with CJC-1295 including increased heart rate and a systemic vasodilatory reaction, and that available clinical data are limited.^{[6,7,8,9,10,11]}

CJC-1295 with DAC at a glance

• A 30-residue peptide: the first 29 residues of human growth hormone-releasing hormone with four changes, D-alanine at 2, glutamine at 8, alanine at 15 and leucine at 27, plus an added lysine 30 whose side chain carries a maleimide and whose C-terminus is an amide. Formula C165H269N47O46, average mass about 3647.2 g/mol, monoisotopic 3645.0155 Da.^[1,12,5]
• The maleimide is the whole point of the suffix DAC, for drug affinity complex. It adds across a free protein thiol, and the resulting thioether has been located by mass spectrometry on the tryptic peptide of serum albumin that contains cysteine 34, the one unpaired cysteine of that protein.^[3,13,14]
• Each of the four substitutions answers a specific chemical liability of the parent sequence: cleavage between residues 2 and 3 by dipeptidyl peptidase IV, rearrangement of asparagine 8 in water, and oxidation of methionine 27. The molecule contains no sulfur and no cysteine of its own.^[15,2,1]
• The name means two different molecules and only the formula settles which. This one, with the arm, is C165H269N47O46, average about 3647.2 g/mol, monoisotopic 3645.0155 Da, PubChem CID 91971820, CAS 446262-90-4. The 29-residue peptide with the same four substitutions and no arm is C152H252N44O42, average about 3367.9 g/mol, monoisotopic 3365.9 Da, PubChem CID 56841945, CAS 863288-34-0; several anti-doping papers call that one CJC-1295 and name this one CJC-1295 with drug affinity complex.^[1,16,4,17]
• No three-dimensional structure exists for this molecule. The deposited structures that its sequence retrieves are the parent hormone bound to its receptor, and one fusion protein whose analogue segment is entirely unmodelled.^[18,19,1]
• Status, in brief: no marketing authorisation in any register searched, and the one registered trial found under the name is recorded as terminated. CJC-1295 is named on the World Anti-Doping Agency 2026 Prohibited List under S2.2.4 as a growth hormone-releasing hormone analogue, prohibited at all times, and the FDA's list of bulk drug substances that may present significant safety risks records a withdrawn nomination for a substance named CJC-1295, stating that the agency has identified serious adverse events associated with it including increased heart rate and a systemic vasodilatory reaction. The regulatory status section above carries the agency's full wording.^{[6,7,8,9,10,11]}

What is CJC-1295 with DAC?

Human growth hormone-releasing hormone is a 44-residue hypothalamic peptide, and its first 29 residues with a C-terminal amide (sermorelin) were long treated as the short form that keeps the parent's activity in a pituitary assay. That fragment has three chemical weaknesses that are well documented and unrelated to each other: plasma dipeptidyl peptidase IV removes the first two residues in one cut, the asparagine at position 8 rearranges in water through a cyclic aminosuccinimide, and the methionine at 27 oxidises.^[15,2,20]

A series of analogues published in 1994 addressed those three liabilities position by position, replacing the amino terminus to stop the protease, residue 8 to slow the rearrangement and residue 27 to remove the oxidisable sulfur, and adding alanine at 15 because that change had already been reported to raise receptor binding affinity. This molecule carries the same logic in its mature form: D-alanine 2, glutamine 8, alanine 15, leucine 27.^[2,15]

What makes it a distinct object rather than one more substituted fragment is the thirty-first atom group, not the thirtieth residue. A lysine was appended and its side chain acylated with 3-maleimidopropionic acid. Maleimides add across thiols, and human plasma offers a large and accessible one: albumin circulates with a single unpaired cysteine. The peptide was described in 2005 by a Montreal company working this chemistry across unrelated sequences, which published the same arm on a glucagon-like peptide-1 analogue (CJC-1131) and on an HIV fusion-inhibitor peptide. Of three maleimido derivatives of the 1-29 fragment prepared and conjugated to human albumin outside the body, the one with the arm at the C-terminus was selected and named CJC-1295.^[5,21,22,23]

So the molecule as supplied is a reagent, and the species that circulates is a protein. That distinction is not a quibble: the analytical literature says it explicitly, that once conjugated the material behaves as a protein of undefined molecular weight and defeats the top-down peptide screens that identify every other peptide in its class. Describing it as a peptide drug is accurate about the vial and wrong about the blood.^[24,14,3]

CJC-1295 with DAC structure and sequence

Read as a graph, the molecule is one linear chain of thirty amino acids with a single branch. Twenty-nine of the residues reproduce the parent hormone's amino-terminal segment, numbered the same way, with four of those positions exchanged. Position 2 is the one departure from L-stereochemistry. Position 30 is the added lysine: its alpha-carboxyl is an amide, and its epsilon-amine carries a three-carbon acyl chain ending in a maleimide ring. There is no cysteine, so the molecule cannot react with itself, and no methionine, so there is nothing in it to oxidise; the only sulfur anywhere in this chemistry arrives from the protein it meets.^[1,12]

The maleimide is a strained, electron-poor double bond between two carbonyls. A thiolate adds across it to give a succinimidyl thioether, which creates a new stereocentre at the ring carbon that took the sulfur, so a conjugate is a pair of diastereomers at that one atom. The ring can also open by hydrolysis after the addition, giving a ring-opened succinamic acid that is no longer able to exchange its thiol; one study found the albumin adduct in exactly that hydrolysed state, at an accurate mass consistent with the opened ring. The arm as drawn in the registry records is the closed, unreacted form, which is the form in the vial and not the form in plasma.^[1,3]

Nothing experimental fixes the shape. Circular dichroism work on close relatives of the 1-29 scaffold reports partial helicity that depends on the solvent, and one study of position-19 variants in that series found helical content in buffer inversely related to in vitro potency, which is a reason not to treat a helix as a feature of the active molecule. For this analogue there is no deposited structure, no calculated conformer and no spectroscopic measurement in the literature read here. What the sequence search does return is instructive about the limits: the parent hormone bound to its receptor, and a botulinum-toxin fusion whose growth hormone-releasing hormone segment, carrying three of these four substitutions, is unobserved along its whole length.^[25,18,19,1]

Set side by side, five molecules in and around this series separate cleanly on mass. Sermorelin is GRF(1-29) amide with no substitutions, monoisotopic 3355.8 Da. CJC-1293 adds only the D-alanine at position 2, so it has the same monoisotopic mass as sermorelin, 3355.8 Da, which is why one laboratory reports the two cannot be told apart by retention time or product-ion spectrum. The no-DAC peptide carries all four substitutions on the same 29 residues and comes out at 3365.9 Da, 10.1 Da above sermorelin, because glutamine for asparagine at 8 and leucine for methionine at 27 together add that much. This molecule is that sequence plus lysine 30 and the maleimidopropionyl arm, monoisotopic 3645.0 Da, a further 279.1 Da. Tesamorelin sits outside the series altogether: the full 44-residue chain with a hexenoyl group on the N-terminal tyrosine, monoisotopic 5132.7 Da, and no covalent arm of any kind.^{[4,26,1,16,12]}

One D-residue, the alanine at position 2; all other stereocentres are L, including the two isoleucines and the threonine, which each carry a second centre in the side chain. The maleimide ring is planar and achiral, and the thioether carbon it generates on reacting with a thiol is a new stereocentre whose configuration nothing in the public record fixes, so a conjugate is a mixture of two diastereomers at that one position. The peptide chain itself is linear with no cyclisation, no lipid arm, no polyethylene glycol and no metal coordination.^[1,12]

What studies on CJC-1295 with DAC show

Each card names the experimental system and what was measured. A result in one system is not evidence about another.

CJC-1295 with DAC compared with CJC-1295 without DAC and Sermorelin

Four things about the 3 compounds most often read beside it, on axes that can be checked: what kind of substance it is, its formula and mass, what public records settle about which substance it is, and the strongest three-dimensional evidence that exists for it. Every figure is the one stated on that compound's own page, which is where it is cited, so the two can never disagree. The table compares no effect, no potency and nothing a compound has been reported to do, and these compounds are not alternatives to one another.

Where the four substitutions and the maleimide arm sit relative to the receptor contact map

The receptor is a class B1 G protein-coupled receptor with an extracellular domain and a seven-helix bundle, and the cryo-EM structure of it bound to the parent hormone shows the ligand as a single continuous helix: the amino terminus buried in the helical bundle, the middle of the chain across the extracellular loops, the C-terminal part against the extracellular domain. That geometry explains the shape of this molecule in a way nothing about the molecule itself does. The positions that matter most for binding cluster in the first eleven residues, which the analogue leaves untouched apart from the stereochemistry at 2; the added lysine and its arm hang off the end that points away from the bundle, which is the end a 66 kDa protein can be attached to without blocking the pocket.^[32,31,5]

Read against that map, the four substitutions fall into three different cases. The D-alanine at 2 occupies a position whose side chain is an ordinary hydrophobic contact and whose inversion did not change measured affinity, while blocking the single peptidase cut that otherwise destroys the chain. Alanine at 15 sits at a position the structure paper explicitly calls substitution-tolerant. Glutamine at 8 and leucine at 27 are the two interesting ones, because asparagine 8 makes a named hydrogen bond to the receptor's second extracellular loop and methionine 27 makes hydrophobic contact with the extracellular domain: both substitutions sit on real contacts, and whether they weaken them has not been measured for this molecule at any receptor.^[32,31,2]

The arm works by thiol chemistry rather than by affinity, and that is the second half of the mechanism. A maleimide adds across a thiolate to give a thioether, so the peptide becomes a permanent appendage of whatever carried the free thiol: in plasma, principally albumin at cysteine 34, the one unpaired cysteine among its thirty-five. Albumin's own long circulation then governs the conjugate rather than the peptide's clearance doing so. Two consequences follow from the chemistry and were both observed. The conjugate stays active, since albumin-conjugated versions of three unrelated peptides retained receptor activation or antiviral potency, so the bond does not hide the business end. And the conjugate is no longer one molecular species, which is why the analytical literature treats it as a protein and why the material recovered from plasma was found with its succinimide ring hydrolysed rather than as drawn.^{[3,13,21,22,23,24]}

What is still unknown about CJC-1295 with DAC

The name is the first problem, and it is not labelling pedantry. The compact side-by-side comparison is in At a glance; what remains here is which records point which way. Several anti-doping laboratories write CJC-1295 for the 29-residue peptide with these four substitutions and no lysine-maleimide, and name the conjugating molecule separately as CJC-1295 with drug affinity complex; one 2021 study lists them as two of its four analytes. PubChem's record for the 29-mer carries CJC-1295 with DAC and DAC:GRF acetate among its synonyms although its formula contains neither the extra lysine nor the maleimide, and the record for this molecule carries the 29-mer's CAS number as a deprecated identifier. A preparation sold as CJC-1295 and examined in 2010 by a doping-control laboratory was found to contain a 29-residue amidated peptide, which is the no-DAC molecule. So a sequence, a mass, a registry number and a product label can each point to a different one of the two, and only the formula settles it.^{[4,17,16,33,1]}

No potency figure for this molecule exists in the public record read here. There is no published affinity at a cloned growth hormone-releasing hormone receptor, no EC50 in a cAMP assay, and no comparison in such an assay against the parent hormone, sermorelin or the no-DAC form. What the discovery paper reports is a growth hormone secretion assay in pituitary cell culture and an area-under-the-curve ratio in rats, both for the conjugate, which cannot separate receptor potency from the carrier's persistence. The structural and mutagenesis evidence for the receptor comes from the parent hormone, never from this analogue.^[5,32,31]

Published tables disagree about the sequence of the no-DAC form, which matters because the DAC form is defined as that sequence plus a residue. One 2016 table prints it as YdADAIFTQSYRKVLAQLSARKLLQDILSR-NH2, with the D-residue marked, while a 2022 table from the same laboratory prints YANAIFTQSYRKVLAQLSARKLLQDILSR-NH2 for the same name and the same monoisotopic mass, which drops the stereochemical marker and reads asparagine where the earlier table has aspartate. The mass given in both is identical, so the later string is a typographic slip rather than a different molecule; the sequence on this page follows the FDA registry's subunit and the PubChem graph, which agree with each other and with the first table.^[4,26,12,1]

What the conjugate actually is in a given sample is not fully characterised. The peptide has been reported bound to a range of plasma proteins rather than albumin alone; the one adduct mapped by mass spectrometry was in the ring-opened state, so the proportions of closed and hydrolysed succinimide are unknown; the new stereocentre created by the thiol addition means a conjugate is at least two diastereomers; and nothing has been deposited structurally for this or any sibling conjugate. Measurement reflects this: the molecule is screened by immunoassay or by immuno-PCR against the intact conjugate, or by mass spectrometry of signature tryptic fragments after digestion, and the one method that reports an undigested mass is the one applied to the free peptide in urine.^{[3,24,14,34,35]}

Key papers on CJC-1295 with DAC

1. 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.

   Jetté L, Léger R, Thibaudeau K, Benquet C, Robitaille M, Pellerin I, Paradis V, van Wyk P, Pham K, Bridon DP (2005), Endocrinology · Synthesis with in vitro stability, cell assay and rodent pharmacokinetics

   The discovery paper, and the only published work on this molecule's own chemistry: it says which maleimido derivative was selected, that the conjugate resists the peptidase and is active in pituitary cell culture, and that it persists in rat plasma. Abstract only, from the company that made it.

2. A method for confirming CJC-1295 abuse in equine plasma samples by LC-MS/MS.

   Timms M, Ganio K, Steel R (2019), Drug Testing and Analysis · Immunoaffinity capture, tryptic digestion and tandem mass spectrometry

   The best direct evidence of the conjugate's chemistry: the added mass of the amidated lysine and its arm located on the albumin tryptic peptide that carries cysteine 34, with the ring-opened state identified by accurate mass. Also the clearest statement of why the molecule is analysed as a protein.

3. Structural basis for activation of the growth hormone-releasing hormone receptor.

   Zhou F, Zhang H, Cong Z, Zhao LH, Zhou Q, Mao C, Cheng X, Shen DD, Cai X, Ma C, Wang Y, Dai A, Zhou Y, Sun W, Zhao F, Zhao S, Jiang H, Jiang Y, Yang D, Xu HE, Zhang Y, Wang MW (2020), Nature Communications · Cryo-EM structure with alanine scanning and molecular dynamics

   The near-atomic structure of the receptor with a peptide in it, and the source for where positions 8, 15 and 27 sit in the contact map. Open access. Read it knowing the ligand is the 44-residue hormone, not this analogue.

4. Enhanced stability and potency of novel growth hormone-releasing factor (GRF) analogues derived from rodent and human GRF sequences.

   Campbell RM, Stricker P, Miller R, Bongers J, Liu W, Lambros T, Ahmad M, Felix AM, Heimer EP (1994), Peptides · Analogue series with stability measurement and two bioassays

   The reason to believe glutamine 8, alanine 15 and leucine 27 are there for isomerisation, affinity and oxidation respectively, measured on a sibling analogue series rather than asserted.

5. Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma.

   Frohman LA, Downs TR, Heimer EP, Felix AM (1989), The Journal of Clinical Investigation · Plasma degradation enzymology

   The enzymology the D-alanine answers: one-step cleavage of the 2-3 bond by dipeptidyl peptidase IV, blocked by a D-residue at position 1 or 2.

6. Qualitative identification of growth hormone-releasing hormones in human plasma by means of immunoaffinity purification and LC-HRMS/MS.

   Knoop A, Thomas A, Fichant E, Delahaut P, Schänzer W, Thevis M (2016), Analytical and Bioanalytical Chemistry · Immunoaffinity LC-HRMS/MS with in vitro and rodent stability

   Open access, and the clearest worked example of the naming problem: it defines CJC-1295 as the 29-residue substituted amide, gives its mass and sequence in a table, and shows that the D-alanine analogues produce no truncated metabolite where sermorelin does.

7. Development and characterization of a glucagon-like peptide 1-albumin conjugate: the ability to activate the glucagon-like peptide 1 receptor in vivo.

   Kim JG, Baggio LL, Bridon DP, Castaigne JP, Robitaille MF, Jetté L, Benquet C, Drucker DJ (2003), Diabetes · Receptor binding and cAMP assay with rodent work

   The platform read on a different sequence: an albumin conjugate of a glucagon-like peptide-1 analogue binding and activating its own cloned receptor, which is the receptor-level evidence this chemistry has and that the GRF version lacks.

References

1. 1.National Center for Biotechnology Information. PubChem Compound Summary for CID 91971820, CJC 1295. PubChem. source · database record
2. 2.Campbell RM, Stricker P, Miller R, Bongers J, Liu W, Lambros T, Ahmad M, Felix AM, Heimer EP. (1994). Enhanced stability and potency of novel growth hormone-releasing factor (GRF) analogues derived from rodent and human GRF sequences. Peptides. 15:489-495. doi:10.1016/0196-9781(94)90211-9 · abstract only
3. 3.Timms M, Ganio K, Steel R. (2019). A method for confirming CJC-1295 abuse in equine plasma samples by LC-MS/MS. Drug Testing and Analysis. 11:1248-1257. doi:10.1002/dta.2599 · full text read
4. 4.Knoop A, Thomas A, Fichant E, Delahaut P, Schänzer W, Thevis M. (2016). Qualitative identification of growth hormone-releasing hormones in human plasma by means of immunoaffinity purification and LC-HRMS/MS. Analytical and Bioanalytical Chemistry. 408:3145-3153. doi:10.1007/s00216-016-9377-3 · full text read
5. 5.Jetté L, Léger R, Thibaudeau K, Benquet C, Robitaille M, Pellerin I, Paradis V, van Wyk P, Pham K, Bridon DP. (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. 146:3052-3058. doi:10.1210/en.2004-1286 · abstract only
6. 6.U.S. Food and Drug Administration. (2026). Drugs@FDA: FDA-Approved Drugs. U.S. Food and Drug Administration. source · database record
7. 7.European Medicines Agency. (2026). Medicines. European Medicines Agency. source · database record
8. 8.Health Canada. (2026). Drug Product Database online query. Health Canada. source · database record
9. 9.U.S. National Library of Medicine. (2005). A Study to Evaluate CJC 1295 in HIV Patients With Visceral Obesity (NCT00267527). ClinicalTrials.gov. source · database record
10. 10.World Anti-Doping Agency. (2026). The 2026 Prohibited List: International Standard. World Anti-Doping Agency. source · full text read
11. 11.U.S. Food and Drug Administration. (2026). Certain Bulk Drug Substances for Use in Compounding that May Present Significant Safety Risks. U.S. Food and Drug Administration. source · full text read
12. 12.US Food and Drug Administration, Global Substance Registration System. Substance record for CJC-1295, UNII 62RC32V9N7. FDA GSRS. source · database record
13. 13.UniProt Consortium. UniProtKB P02768 (ALBU_HUMAN), Albumin. UniProtKB. source · database record
14. 14.Timms M, Cawley A, Steel R. (2026). Detection of CJC-1295 in Equine Plasma by ELISA. Drug Testing and Analysis. doi:10.1002/dta.70171 · abstract only
15. 15.Frohman LA, Downs TR, Heimer EP, Felix AM. (1989). Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma. The Journal of Clinical Investigation. 83:1533-1540. doi:10.1172/JCI114049 · abstract only
16. 16.National Center for Biotechnology Information. PubChem Compound Summary for CID 56841945, L-tyrosyl-D-alanyl-..-L-argininamide. PubChem. source · database record
17. 17.Memdouh S, Gavrilović I, Ng K, Cowan D, Abbate V. (2021). Advances in the detection of growth hormone releasing hormone synthetic analogs. Drug Testing and Analysis. 13:1871-1887. doi:10.1002/dta.3183 · abstract only
18. 18.Zhou F, Zhang H, Cong Z, Zhao L, Zhou Q, Mao C, Cheng X, Shen D, Cai X, Ma C, Wang Y, Dai A, Zhou Y, Sun W, Zhao F, Zhao S, Jiang H, Jiang Y, Yang D, Xu HE, Zhang Y, Wang M. (2020). Cryo-EM structure of the human growth hormone-releasing hormone receptor-Gs protein complex. Protein Data Bank entry 7CZ5. doi:10.2210/pdb7CZ5/pdb · database record
19. 19.Masuyer G, Davies JR, Moore K, Chaddock JA, Ravi Acharya K. (2015). Crystal structure of SXN101959, a Clostridium botulinum neurotoxin type D derivative and targeted secretion inhibitor. Protein Data Bank entry 5BQM. doi:10.2210/pdb5BQM/pdb · database record
20. 20.UniProt Consortium. UniProtKB P01286 (SLIB_HUMAN), Somatoliberin. UniProtKB. source · database record
21. 21.Léger R, Thibaudeau K, Robitaille M, Quraishi O, van Wyk P, Bousquet-Gagnon N, Carette J, Castaigne JP, Bridon DP. (2004). Identification of CJC-1131-albumin bioconjugate as a stable and bioactive GLP-1(7-36) analog. Bioorganic & Medicinal Chemistry Letters. 14:4395-4398. doi:10.1016/j.bmcl.2004.06.066 · abstract only
22. 22.Kim JG, Baggio LL, Bridon DP, Castaigne JP, Robitaille MF, Jetté L, Benquet C, Drucker DJ. (2003). Development and characterization of a glucagon-like peptide 1-albumin conjugate: the ability to activate the glucagon-like peptide 1 receptor in vivo. Diabetes. 52:751-759. doi:10.2337/diabetes.52.3.751 · abstract only
23. 23.Stoddart CA, Nault G, Galkina SA, Thibaudeau K, Bakis P, Bousquet-Gagnon N, Robitaille M, Bellomo M, Paradis V, Liscourt P, Lobach A, Rivard ME, Ptak RG, Mankowski MK, Bridon D, Quraishi O. (2008). Albumin-conjugated C34 peptide HIV-1 fusion inhibitor: equipotent to C34 and T-20 in vitro with sustained activity in SCID-hu Thy/Liv mice. The Journal of Biological Chemistry. 283:34045-34052. doi:10.1074/jbc.M805536200 · abstract only
24. 24.Timms M, Ganio K, Forbes G, Bailey S, Steel R. (2019). An immuno polymerase chain reaction screen for the detection of CJC-1295 and other growth-hormone-releasing hormone analogs in equine plasma. Drug Testing and Analysis. 11:804-812. doi:10.1002/dta.2554 · abstract only
25. 25.Friedman AR, Ichhpurani AK, Moseley WM, Alaniz GR, Claflin WH, Cleary DL, Prairie MD, Krueger WC, Frohman LA, Downs TR, et al. (1992). Growth hormone-releasing factor analogs with hydrophobic residues at position 19. Effects on growth hormone releasing activity in vitro and in vivo, stability in blood plasma in vitro, and secondary structure. Journal of Medicinal Chemistry. 35:3928-3933. doi:10.1021/jm00099a021 · abstract only
26. 26.Thomas A, Thilmany S, Hofmann A, Thevis M. (2022). Probing for peptidic drugs (2-10 kDa) in doping control blood samples. Analytical Science Advances. 3:235-243. doi:10.1002/ansa.202200027 · full text read
27. 27.Teichman SL, Neale A, Lawrence B, Gagnon C, Castaigne JP, Frohman LA. (2006). 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. The Journal of Clinical Endocrinology and Metabolism. 91:799-805. doi:10.1210/jc.2005-1536 · abstract only
28. 28.Ionescu M, Frohman LA. (2006). Pulsatile secretion of growth hormone (GH) persists during continuous stimulation by CJC-1295, a long-acting GH-releasing hormone analog. The Journal of Clinical Endocrinology and Metabolism. 91:4792-4797. doi:10.1210/jc.2006-1702 · abstract only
29. 29.Sackmann-Sala L, Ding J, Frohman LA, Kopchick JJ. (2009). 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 Hormone & IGF Research. 19:471-477. doi:10.1016/j.ghir.2009.03.001 · abstract only
30. 30.Alba M, Fintini D, Sagazio A, Lawrence B, Castaigne JP, Frohman LA, Salvatori R. (2006). Once-daily administration of CJC-1295, a long-acting growth hormone-releasing hormone (GHRH) analog, normalizes growth in the GHRH knockout mouse. American Journal of Physiology. Endocrinology and Metabolism. 291:E1290-E1294. doi:10.1152/ajpendo.00201.2006 · abstract only
31. 31.Lefrançois L, Gaudreau P. (1994). Identification of receptor-binding pharmacophores of growth-hormone-releasing factor in rat adenopituitary. Neuroendocrinology. 59:363-370. doi:10.1159/000126679 · abstract only
32. 32.Zhou F, Zhang H, Cong Z, Zhao LH, Zhou Q, Mao C, Cheng X, Shen DD, Cai X, Ma C, Wang Y, Dai A, Zhou Y, Sun W, Zhao F, Zhao S, Jiang H, Jiang Y, Yang D, Xu HE, Zhang Y, Wang MW. (2020). Structural basis for activation of the growth hormone-releasing hormone receptor. Nature Communications. 11:5205. doi:10.1038/s41467-020-18945-0 · full text read
33. 33.Henninge J, Pepaj M, Hullstein I, Hemmersbach P. (2010). Identification of CJC-1295, a growth-hormone-releasing peptide, in an unknown pharmaceutical preparation. Drug Testing and Analysis. 2:647-650. doi:10.1002/dta.233 · abstract only
34. 34.Coppieters G, Deventer K, Polet M, Van Eenoo P, Judák P. (2022). An antibody-free, ultrafiltration-based assay for the detection of growth hormone-releasing hormones in urine at low pg/mL concentrations using nanoLC-HRMS/MS. Journal of Pharmaceutical and Biomedical Analysis. 214:114726. doi:10.1016/j.jpba.2022.114726 · abstract only
35. 35.Thomas A, Walpurgis K, Thevis M. (2024). Chromatographic-mass spectrometric analysis of peptidic analytes (2-10 kDa) in doping control urine samples. Journal of Mass Spectrometry. 59:e4996. doi:10.1002/jms.4996 · abstract only
36. 36.Bongers J, Lambros T, Ahmad M, Heimer EP. (1992). Kinetics of dipeptidyl peptidase IV proteolysis of growth hormone-releasing factor and analogs. Biochimica et Biophysica Acta. 1122:147-153. doi:10.1016/0167-4838(92)90317-7 · abstract only