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Mod GRF 1-29

Sermorelin, Growth Hormone Releasing Hormone (1-29), hGRF(1-29)NH2

A synthetic peptide analog of growth hormone-releasing hormone that stimulates the pituitary gland to secrete growth hormone.

Quick Stats
Studies 227
Trials 47
Formula C149H246N44O42S
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Utility 3
pubmed Feb 1, 1986

Does growth hormone releasing factor desensitize the somatotroph? Interpretation of responses of growth hormone during and after 10-hour infusion of GRF 1-29 amide in man.

Davis. J R JR; Sheppard. M C MC; Shakespear. R A RA; Lynch. S S SS; Clayton. R N RN

A short study gave four healthy men a steady 10‑hour infusion of the growth‑hormone‑releasing peptide GRF‑1‑29. GH levels rose in pulses during the infusion, but after the infusion the same dose given as a quick shot produced a weaker and inconsistent GH response, hinting that the pituitary may become less responsive after continuous exposure.

Utility 3
pubmed Mar 1, 1986

Influence of dopaminergic, adrenergic and cholinergic blockade and TRH administration on GH responses to GRF 1-29.

Jordan. V V; Dieguez. C C; Lafaffian. I I; Rodriguez-Arnao. M D MD; Gomez-Pan. A A; Hall. R R; Scanl...

The study shows that when you take the growth‑hormone‑releasing peptide GRF‑1‑29, drugs that block dopamine or alpha‑adrenergic receptors don’t change its ability to boost GH, but drugs that block acetylcholine (like atropine) do blunt the GH surge. Thyrotropin‑releasing hormone (TRH) also doesn’t interfere with GRF‑1‑29’s effect.

Utility 3
pubmed Dec 31, 1986

Strategies in the design of synthetic agonists and antagonists of growth hormone releasing factor.

Coy. D H DH; Murphy. W A WA; Lance. V A VA; Heiman. M L ML

Researchers tested many tiny changes to the first part of the growth‑hormone‑releasing peptide (GRF‑1‑29). Swapping some natural amino acids for their mirror‑image (D‑) versions made the peptide work better, while adding extra rigidity or other unusual building blocks usually stopped it from working.

Utility 3
pubmed 1988

Subcutaneous treatment with growth hormone-releasing hormone for short stature.

Hernández. M M; Fragoso. J J; Barrio. R R; Argente. J J; Arilla. E E

Giving the peptide GRF‑1‑29 (a short version of growth‑hormone‑releasing hormone) to 11 short‑stature kids for six months made them grow faster, even though their overall GH and IGF‑I levels didn’t change much. The treatment was well‑tolerated and didn’t alter the normal daily GH pulse pattern.

Utility 3
pubmed 1988

Applications of BOP reagent in solid phase synthesis. Advantages of BOP reagent for difficult couplings exemplified by a synthesis of [Ala 15]-GRF(1-29)-NH2.

Fournier. A A; Wang. C T CT; Felix. A M AM

The study shows that using the BOP chemical reagent makes it easier and faster to build the GRF‑1‑29 peptide on a solid support compared to older methods like DCC. Most amino acids can be added in a single step, giving higher yields and good purity, while a few tricky spots (like Asn) still need extra steps. The method also works with unprotected hydroxy‑amino acids and tyrosine, but only for a short number of cycles.

Utility 3
pubmed 1986

Testing with growth hormone-releasing factor (GRF(1-29)NH2) and somatomedin C measurements for the evaluation of growth hormone deficiency.

Ranke. M B MB; Gruhler. M M; Rosskamp. R R; Brügmann. G G; Attanasio. A A; Blum. W F WF; Bieric...

The study shows that a single IV dose of growth‑hormone‑releasing factor (GRF‑1‑29) reliably triggers a GH surge in healthy people and can be used to spot growth‑hormone deficiency. A GH level above 10 ng/ml after the test is considered normal, and the shorter GRF‑1‑29 works just as well as the longer GRF‑1‑40.

Utility 3
pubmed 1987

Differential effects of N-terminal modifications on the biological potencies of growth hormone releasing factor analogues with varying chain lengths.

Coy. D H DH; Murphy. W A WA; Lance. V A VA; Heiman. M L ML

The study shows that cutting off the tail end of the growth‑hormone‑releasing factor (GRF) peptide makes it much weaker, and only a few tweaks to the front end can partly rescue activity—but even the best‑modified short versions are still far less effective than the full‑length 1‑29 peptide.

Utility 3
pubmed 1987

Characteristics of growth hormone response to the administration of growth hormone-releasing hormone (GRF) in the lamb.

Barenton. B B; Duclos. M M; Diaz. J J; Deletang. F F; Dulor. J P JP; Blanchard. M M; Charrier. J J

In baby and teen lambs, a single shot of growth hormone‑releasing hormone (GRF‑1‑29) quickly spikes growth hormone levels, and doing this every day for three weeks makes the response even stronger. The hormone works the same whether you use the short (1‑29) or longer (1‑44) version, and the pituitary doesn’t get used up or stop responding.

Utility 3
pubmed 1986

Response of growth hormone release to human growth hormone-releasing factor and its analogs in the bovine.

Hodate. K K; Johke. T T; Ohashi. S S

In baby cows, the short version of the growth‑hormone‑releasing factor (GRF 1‑29) works just as well as the longer version (GRF 44), and a tiny tweak—adding a D‑alanine at position 2—makes it even stronger and longer‑lasting. This hints that the shorter peptide could be enough for humans, and the D‑Ala2 version might need a lower dose for the same effect.

Utility 3
pubmed Sep 14, 1986

Amphiphilic growth hormone releasing factor (GRF) analogs: peptide design and biological activity in vivo.

Tou. J S JS; Kaempfe. L A LA; Vineyard. B D BD; Buonomo. F C FC; Della-Fera. M A MA; Baile. C A CA

Scientists tweaked the first 29 building blocks of the natural growth‑hormone‑releasing hormone to make it more water‑friendly on one side and fat‑friendly on the other (amphiphilic). The new versions, with up to eight changes, gave a stronger boost in growth hormone when injected into sheep compared to an older version of the peptide.

Utility 3
pubmed 1985

Structure-activity studies on the N-terminal region of growth hormone releasing factor.

Coy. D H DH; Murphy. W A WA; Sueiras-Diaz. J J; Coy. E J EJ; Lance. V A VA

Scientists tweaked the first few building blocks of the growth‑hormone‑releasing peptide (GRF‑1‑29) and found that swapping them for mirror‑image (D‑) amino acids can make the peptide 12‑ to 38‑fold more powerful at triggering growth hormone release in rats. Some specific changes (like D‑Ala at position 2) were especially effective, while others killed the activity.

Utility 3
pubmed 1995

Pegylated peptides. IV. Enhanced biological activity of site-directed pegylated GRF analogs.

Felix. A M AM; Lu. Y A YA; Campbell. R M RM

Scientists attached polyethylene glycol (PEG) chains to a short version of the growth‑hormone‑releasing hormone (GRF‑1‑29) to see if the peptide would still work. They found that where you put the PEG matters: attaching it to the ends of the peptide (especially the C‑terminal end) keeps the hormone‑releasing activity, while attaching it to the front or certain middle spots makes it weaker.

Utility 3
pubmed 1994

Peptide synthesis catalyzed by the Glu/Asp-specific endopeptidase. Influence of the ester leaving group of the acyl donor on yield and catalytic efficiency.

Bongers. J J; Liu. W W; Lambros. T T; Breddam. K K; Campbell. R M RM; Felix. A M AM; Heimer. E P EP

Scientists showed that an enzyme called GSE from Bacillus can stitch together a modified growth‑hormone‑releasing peptide (GRF‑1‑29) more efficiently than the older V8 protease, especially when the right chemical “leaving group” is attached to the donor piece. This reduces unwanted breakdown and boosts the amount of final product.

Utility 3
pubmed 1992

Defective response of plasma growth hormone to growth hormone releasing factor in growth hormone deficient children.

Ko. F Y FY; Chen. W P WP; Lin. C Y CY

Giving a single dose of the peptide GRF‑1‑29 to kids triggers a spike in their blood growth hormone about 45 minutes later. Normal kids reach high levels, while growth‑hormone‑deficient kids still respond but to a much lower peak. About one‑fifth of the deficient kids barely responded, hinting their problem might lie in the brain rather than the pituitary.

Utility 3
pubmed 1991

1H NMR analysis and in vitro bioactivity of Leu27-bGRF(1-29)NH2 and its D-Ala2 and des-(Tyr1-Ala2)-analogs.

Kloosterman. D A DA; Scahill. T A TA; Hillman. R M RM; Cleary. D L DL; Kubiak. T M TM

The study compared three versions of a bovine growth‑hormone‑releasing peptide. The full‑length peptide (I) was the most active, a version missing the first two amino acids (IV) was almost dead, and a version with a D‑Ala change at position 2 (III) was almost as active as the full‑length peptide. The shape of the peptides in a test solution didn’t explain the activity differences, suggesting the very start of the molecule matters for binding to the receptor.

Utility 3
pubmed 1992

Semisynthesis of human growth hormone-releasing factors by alpha-amidating enzyme catalyzed oxidation of glycine-extended precursors.

Bongers. J J; Felix. A M AM; Campbell. R M RM; Lee. Y Y; Merkler. D J DJ; Heimer. E P EP

Scientists showed a reliable way to make the growth‑hormone‑releasing peptide GRF‑1‑29 (and related versions) using an enzyme that adds an amide group. The process gives about 75% yield and the resulting peptide works just as well as the natural hormone in lab tests.

Utility 3
pubmed 1990

Effects of GRF (1-29) NH2 on short-term memory: neuroendocrine and neuropsychological assessment in healthy young subjects.

Alvarez. X A XA; Cacabelos. R R

A single IV dose of 150 µg GRF‑1‑29 (the short fragment of growth‑release‑factor) helped healthy young adults remember more words two hours later compared to a saline placebo. The memory boost was seen in both people with high and low natural growth‑hormone levels, though those with higher baseline GH showed a bigger hormone spike after the injection.