Mod GRF (1-29) (CJC-1295 without DAC) / Studies

Synthetic analog · 29 amino acids · 3,367.9 Da

Mod GRF (1-29) (CJC-1295 without DAC) studies and research data

PepBank has no study results for CJC-1295 no DAC yet. Data as of 2026-10-30.

Searches 0 results and 2 papers. Newer studies from Europe PMC

Results in people

0% of 0 results

Results in animals

0% of 0 results

Results in lab cells

0% of 0 results

From computer models

0% of 0 results

The molecule

CJC-1295 no DAC identity

Identifiers, parent molecule, targets and development stage, from curated data.

Mod GRF (1-29) is a synthetic 29-residue GHRH analogue. Its sequence has D-Ala2, Gln8, Ala15 and Leu27, with a C-terminal amide. FDA calls this structure CJC-1295 (free base). CJC-1295 DAC has an additional modified lysine and is a separate active moiety. The acetate salt is also a separate bulk substance. The no-DAC names occur in retail and community sources. FDA reports no available UNII for this free base. GHRH receptor agonism is proposed from its analogue class. The selected ClinicalTrials.gov name query returned no records.

Kind: Synthetic analog · 29 residues
Identifiers: PubChem CID56841945 (opens in a new tab)CAS446036-97-1
Parent: Analog of Somatorelin, human GHRH(1-44) · residues 32-60UniProt P01286 defines mature somatoliberin at precursor positions 32-75. Its first 29 residues correspond to positions 32-60. Comparison with the FDA sequence gives D-Ala2, Gln8, Ala15 and Leu27.
Development: No known clinical developmentThe selected ClinicalTrials.gov name query returned zero records on 2026-10-13. Only the count was checked. No study records were read. This does not exclude trials under other names. The development phase and developer remain unknown for this no-DAC substance. Source (opens in a new tab)

Targets

Molecular targets with action and evidence source
Target	Action	Evidence
Growth hormone-releasing hormone receptorGHRHRQ02643 (opens in a new tab)	Agonist	proposedSource (opens in a new tab)

Sequence and structure

Residues, differences from the parent, calculated properties and 3D structure. Source values and calculated values are shown separately.

Sequence

29 amino acids · 5 modifications

H-

YDAIFTSY

RKVLQLSAR

KLLQDISR

Alignment to Somatorelin, human GHRH(1-44)

Calculated from the two sequences. Curated notes are shown as given.

25 of 29 aligned residues identical (86%) · 3 substitutions · 1 non-canonical residue · 1 modified residue · Somatorelin, human GHRH(1-44) 1–29

Top row: Somatorelin, human GHRH(1-44) (parent)
Bottom row: Mod GRF (1-29) (CJC-1295 without DAC)

YDAIFTSY

RKVLQLSAR

KLLQDIS

Same as parent
Substituted
Non-canonical or D-form
Added
Gap
Modified side chain or end
Parent context

Differences from the parent

1Parent 2 · analog 2Ala → D-Ala · D-amino acidL-Ala replaced by D-Ala. D-alanine in place of L-Ala2.
2Parent 8 · analog 8Asn → Gln · SubstitutionAsn8 replaced by Gln8. Asn8 of native hGRF(1-29) replaced by Gln.
3Parent 15 · analog 15Gly → Ala · SubstitutionGly15 replaced by Ala15. Gly15 of native hGRF(1-29) replaced by Ala.
4Parent 27 · analog 27Met → Leu · SubstitutionMet27 replaced by Leu27. Met27 of native hGRF(1-29) replaced by Leu.
5Parent 29 · analog 29Arg, modified · C-terminal amideC-terminal argininamide.

Basis: UniProt P01286 defines mature somatoliberin at precursor positions 32-75. Its first 29 residues correspond to positions 32-60. Comparison with the FDA sequence gives D-Ala2, Gln8, Ala15 and Leu27.

Calculated from the two sequences with @pepdb/chem alignToParent (ungapped unless a gap scores higher). The record’s curated notes are shown as given.

Properties

From identity sources

Formula: C₁₅₂H₂₅₂N₄₄O₄₂
Molecular weight: 3,367.9 g/mol
Monoisotopic mass: 3,365.8936 Da

PubChem CID 56841945(opens in a new tab)retrieved 2026-10-13
Curated substitution check against mature somatoliberin 1-29(opens in a new tab)retrieved 2026-10-13
Curated FDA PCAC briefing document 2024-12-04, Table 1 (CJC-1295 (free base))(opens in a new tab)retrieved 2026-10-13

Calculated from the sequence

pKa set

Average mass: 3,367.94 Da; Sum of ExPASy residue masses + water + C-amide · ExPASy Compute pI/Mw; FindMod
Monoisotopic mass: 3,365.8935 Da; Sum of ExPASy residue masses + water + C-amide · ExPASy FindMod
Isoelectric point (pI): 10.95; pH of zero net charge, EMBOSS pKa set · EMBOSS iep, Epk.dat
Net charge at pH 7.4: 3.94; Henderson-Hasselbalch, EMBOSS pKa set · EMBOSS iep, Epk.dat
GRAVY (hydropathy): −0.079; Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982; Negative: hydrophilic on average.
Extinction coefficient, 280 nm (Cys reduced): 2,980 M⁻¹ cm⁻¹; 5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam); No Trp: ExPASy reports more than 10 % error without Trp.
Instability index: 46.92; Dipeptide instability weights (DIWV) · Guruprasad et al. 1990; Above 40: classed as possibly unstable (ExPASy).
Aliphatic index: 117.9; Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
Boman index: 1.87 kcal/mol; Mean solubility value (negated) · Boman 2003; 2.48 or below: lower protein-binding potential (Boman).
Hydrophobic moment (μH): 0.611; Eisenberg scale, 100° per residue, best 11-residue window · Eisenberg et al. 1982, 1984
pI with each pKa set: EMBOSS 10.95Bjellqvist (ExPASy) 10.43IPC peptide 10.80IPC protein 10.72

D-amino acids have the same mass and charge as L forms. Hydrophobicity scales were measured on L forms.
Defined and validated for proteins; use with care for short peptides.
Assumes an ideal alpha helix. Many short peptides are not helical.

@pepdb/chem 0.2.0 · EMBOSS pKa set · ExPASy residue masses

Net charge by pH

pI 10.95 · Net charge at pH 7.4: 3.94

Point or use arrow keys

Henderson-Hasselbalch, EMBOSS pKa set, C-amide. Calculated, not measured.

Show as table

pH	Net charge
0	6.00
1	6.00
2	5.98
3	5.78
4	4.89
5	4.15
6	4.01
7	3.98
8	3.78
9	3.11
10	1.87
11	−0.09
12	−1.58
13	−3.26
14	−3.91

Composition

Hydrophobic41% (12)A I L V
Aromatic10% (3)F Y
Positive17% (5)K R
Negative7% (2)D
Polar24% (7)Q S T

29 residues. Each residue counts in one class; F and W count as aromatic.

A Ala4 · 14%

I Ile2 · 7%

L Leu5 · 17%

M Met0 · 0%

V Val1 · 3%

F Phe1 · 3%

W Trp0 · 0%

Y Tyr2 · 7%

H His0 · 0%

K Lys2 · 7%

R Arg3 · 10%

D Asp2 · 7%

E Glu0 · 0%

N Asn0 · 0%

Q Gln3 · 10%

S Ser3 · 10%

T Thr1 · 3%

C Cys0 · 0%

G Gly0 · 0%

P Pro0 · 0%

3D structure

PredictedAlphaFold DB · P01286

Loads the 3D viewer (3Dmol.js, about 150 KB) and the model file from AlphaFold DB (EMBL-EBI).

2D structure

Mod GRF (1-29) (CJC-1295 without DAC) has 29 residues. A full-atom drawing is hard to read at this size; the sequence view is the reference.

SMILES fromPubChem CID 56841945(opens in a new tab)

CC[C@H](C)[C@@H](C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC2=CC=C(C=C2)O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(=O)N)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CO)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N)NC(=O)[C@H](C)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H](C)NC(=O)[C@H](CC3=CC=C(C=C3)O)N

Helical wheel

An ideal alpha-helix projection. It shows where the hydrophobic residues fall if the peptide folds as a helix. It does not show that it does.

μH, residues shown: 0.189
μH, best 11-residue window: 0.611
Arrow direction: 64°
Residues: 29 · 2 rings of 18

HydrophilicHydrophobic

Eisenberg consensus (normalized) scale · + K, R · − D, E

Assumes an ideal α-helix: 100° per residue, 3.6 residues per turn. The arrow is the mean hydrophobic moment (Eisenberg et al. 1984) and points at the hydrophobic face.

Show as table

Position	Residue	Angle	Eisenberg consensus (normalized)
1	Y	0°	0.26
2	A	100°	0.62
3	D	200°	-0.90
4	A	300°	0.62
5	I	40°	1.38
6	F	140°	1.19
7	T	240°	-0.05
8	Q	340°	-0.85
9	S	80°	-0.18
10	Y	180°	0.26
11	R	280°	-2.53
12	K	20°	-1.50
13	V	120°	1.08
14	L	220°	1.06
15	A	320°	0.62
16	Q	60°	-0.85
17	L	160°	1.06
18	S	260°	-0.18
19	A	0°	0.62
20	R	100°	-2.53
21	K	200°	-1.50
22	L	300°	1.06
23	L	40°	1.06
24	Q	140°	-0.85
25	D	240°	-0.90
26	I	340°	1.38
27	L	80°	1.06
28	S	180°	-0.18
29	R	280°	-2.53

Results by area

CJC-1295 no DAC results by year and outcome

Counts are exact and come from studies that gave the peptide.

Studies by year

No study has results about Mod GRF (1-29) (CJC-1295 without DAC) yet.

Studies
Human
Animal
Lab
Computer model

Studies2 in all, 2019 to 2026

Studies with resultsnone yet

Retracted studies are left out. A study with results in two classes counts in both.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

What the studies measured

People first in each area, then animals, then lab cells. Counts are exact and come from studies that gave the peptide.

No study of CJC-1295 no DAC has results in PepBank yet.

Trials and papers

CJC-1295 no DAC trials

Registered trials that test the peptide, with phase, status and dates. A dot marks trials with posted results.

StatusPhase

0 trials match. Highest phase first. Data from ClinicalTrials.gov.

No trial matches these filters.

Papers

Studies on this peptide. Some have results. The others have none yet.

Sort

Design

2 studies match. Retracted studies are left out.

No study on this page has a result for this peptide.

No result for Mod GRF (1-29) (CJC-1295 without DAC) (2 studies on this page)

These studies name Mod GRF (1-29) (CJC-1295 without DAC) but give no result for it (for example, the results concern another peptide in the study).

PubMed tag: none · 2019

5 results

Glycine-modified growth hormone secretagogues identified in seized doping material.

Gajda et al. 2019Drug testing and analysiscited by 5

PMID 30136411DOI 10.1002/dta.2489PUB-30136411

Full text at the publisher5 results

Publisher page See results (5)

PubMed tag: review-article, Review · 2026

The emerging landscape of performance-enhancing peptides modulating GH-IGF1 axis: bridging the gap between clinical evidence and patient self-administration.

Dominikowski et al. 2026Frontiers in endocrinology

PMID 42395176PMC13322892DOI 10.3389/fendo.2026.1822475PUB-42395176

CC BY

Download PDF

Newer studies

PepBank reads each paper before it shows the results. This search looks in Europe PMC for newer papers that PepBank has not read yet.

Mod GRF (1-29) (CJC-1295 without DAC) studies: 0 papers with results

No paper with results is linked to this peptide.

Status and safety

Regulatory and safety

Approval and sport status, and the safety outcomes reported in study results. Laws and labels change, so check the regulator for the current status.

Regulatory status by jurisdiction, with date and source
Jurisdiction	Body	Status	As of	Source
US	FDA	FDA states that none of the evaluated CJC-1295 bulk substances is a component of an FDA-approved drug. An openFDA active-ingredient search for CJC-1295 returned no match. The FDA safety page lists CJC-1295 among withdrawn nominations. Its safety statement does not distinguish DAC from no-DAC. Do not assign those reported events to this free base alone.	13 Oct 2026	fda.gov (opens in a new tab)
EU	EMA	No CJC-1295, Mod GRF or modified GRF match was found in the cited EMA medicines and orphan designation files on 2026-10-13. These files do not establish the absence of every national approval.	13 Oct 2026	ema.europa.eu (opens in a new tab)
Sport	WADA	Banned in sport (WADA S2.2.4) The current WADA web list links the 2026 PDF.	2026 List	wada-ama.org (opens in a new tab)

Safety outcomes

Reported effects from study results.

No study results yet

No safety results yet. That does not mean the peptide is safe.

Doses studied

The doses that these studies used. They are not recommendations.

No dose was reported in the study results.

PepBank is a research reference. Talk to a doctor before you use any peptide.

Data

Data and API

Data version, change history and code for this peptide.

Data version 30856030 Oct 2026

Peptide

Peptide id: PEP-000010
Peptide version: 10
Peptide hash: 702b53002f5fbb61…
Data version: 308560

Latest changes

27 Oct 2026UpdatedData version 256731
22 Oct 2026UpdatedData version 254552
21 Oct 2026UpdatedData version 213644
14 Oct 2026UpdatedData version 212213
14 Oct 2026UpdatedData version 198210
14 Oct 2026UpdatedData version 194711

For developers

curl -s https://pepbank.io/v1/briefs/mod-grf-1-29

Evidence summary for Mod GRF (1-29) (CJC-1295 without DAC): counts by class, key results with sources, notices, data version.

Peptide as JSON Evidence summary as JSON

Mod GRF (1-29) (CJC-1295 without DAC) studies and research data

CJC-1295 no DAC identity

Targets

Sequence and structure

Sequence

Alignment to Somatorelin, human GHRH(1-44)

Properties

Net charge by pH

Composition

3D structure

2D structure

Helical wheel

CJC-1295 no DAC results by year and outcome

What the studies measured

CJC-1295 no DAC trials

Papers

Glycine-modified growth hormone secretagogues identified in seized doping material.

The emerging landscape of performance-enhancing peptides modulating GH-IGF1 axis: bridging the gap between clinical evidence and patient self-administration.

Newer studies

Mod GRF (1-29) (CJC-1295 without DAC) studies: 0 papers with results

Regulatory and safety

Doses studied

Data and API

Peptide

Latest changes

For developers

Related peptides

CJC-1295 no DAC results by year and outcome

CJC-1295 no DAC trials

Papers

Glycine-modified growth hormone secretagogues identified in seized doping material.

The emerging landscape of performance-enhancing peptides modulating GH-IGF1 axis: bridging the gap between clinical evidence and patient self-administration.

Regulatory and safety

Doses studied

Data and API

Peptide

Latest changes

For developers