IGF-1 DES

IGF-1 DES at a Glance

IGF-1 DES, or des(1-3)IGF-I, is IGF-1 with the first three amino acids removed — a truncation that sharply reduces its affinity for the IGF-binding proteins, leaving more of it free to act at the receptor. Like LR3 it originated as a laboratory tool rather than a therapeutic, and it has never been developed as a human medicine. It is injected as a research chemical, and its approved relative mecasermin is the only place a real safety and efficacy record for IGF-1 exists.

History & Development

des(1-3)IGF-I is IGF-1 with the first three amino acids removed. That deletion makes it far more potent, and for exactly the reason that makes it hard to control.

First described	Not established in the sources consulted for this section
Discovered / synthesised by	Not established in the sources consulted for this section
Institution	Not established in the sources consulted for this section
Origin	IGF-1 variant lacking the N-terminal tripeptide - loss of Glu3 greatly reduces IGF-binding-protein affinity
Key patent	Not established in the sources consulted for this section
Assignee	Not established in the sources consulted for this section
Development status	Research protein - no human trials; never approved

Discovery

Circulating IGF-1 is almost entirely bound to IGF-binding proteins, which act as a reservoir and a brake: bound IGF-1 cannot engage its receptor, so the binding proteins govern how much is active at any moment.

des(1-3)IGF-I removes that brake. Losing the N-terminal tripeptide - Glu3 in particular - sharply reduces IGFBP affinity, so far more of the peptide stays free and receptor-available. It is a fully active IGF-1 receptor agonist with the regulatory system stripped out.

That is why it is more potent, and why the potency is the concern. The binding proteins are not an inefficiency to engineer around; they are the control mechanism. A variant that evades them produces unopposed IGF-1R signalling - and the approved IGF-1 product, mecasermin, shows in its own label that clearance depends inversely on IGFBP-3, meaning its labelled risks are plausibly worse rather than better for an IGFBP-evading variant.

Development & ownership

There is no development programme and no human trial of des(1-3)IGF-I of any kind. Its literature is preclinical - muscle PI3K/Akt/p70-S6K signalling and animal work - and it also carries weak insulin-receptor cross-reactivity, which is the basis of the hypoglycaemia concern.

How it reached the market

It reached consumers directly from the laboratory, sold as an injectable for muscle growth. What is being bought is a molecule engineered to bypass the body’s own control on a growth-signalling pathway, with no human safety data, no established dose, and a mechanism that makes the known risks of approved IGF-1 more likely rather than less.

What It's Used For

IGF-1 DES — properly des(1-3)IGF-I — is human insulin-like growth factor-1 (a 70-residue, ~7.6 kDa single-chain protein) with its first three N-terminal amino acids, glycine-proline-glutamate, removed. Losing the glutamate at position 3 cripples its binding to the IGF-binding proteins (IGFBPs) that normally sequester circulating IGF-I, so more of the peptide stays free to activate the type-1 IGF receptor. That single change makes it roughly ten-fold more potent than IGF-I in cultured cells and about 2–3× more potent in animals ^{1,2,27Reference 1Ballard FJ et al. · 1996ReviewDes(1-3)IGF-I: a truncated form of insulin-like growth factor-I — reviewView study →Reference 2Walton PE et al. · 1995AnimalIn vivo actions of IGF analogues with poor affinities for IGFBPs: metabolic and growth effects in pigs of different ages and GH responsiveness — animal (pig) reviewView study →Reference 27Simes JM et al. · 1991In vitroThe effects of IGF-I, IGF-II and des(1-3)IGF-I, a potent IGF analogue, on growth hormone and IGF-binding protein secretion from cultured rat anterior pituitary cells — in vitroView study →}.

It is not purely a lab invention: it occurs naturally in bovine colostrum, human brain and porcine uterus, and is generated from IGF-I in serum by an acid protease ^{1,4,25Reference 1Ballard FJ et al. · 1996ReviewDes(1-3)IGF-I: a truncated form of insulin-like growth factor-I — reviewView study →Reference 4Yamamoto H et al. · 1994In vitroGeneration of des-(1-3) insulin-like growth factor-I in serum by an acid protease — in vitroView study →Reference 25Yamamoto H et al. · 1995AnimalEnzymatic conversion of IGF-I to des(1-3)IGF-I in rat serum and tissues — animal (rat) / biochemicalView study →}.

The most important fact here is what that potency figure is and is not. It is a binding measurement, made against IGFBP-rich systems — not a demonstration that anything works better in a person. The entire efficacy literature for des(1-3)IGF-I is preclinical: cell culture, transgenic mice, and osmotic-pump infusion studies in rats, pigs, goats and lambs, much of it from 1990s cell-biology and animal-science groups rather than clinical research. No human efficacy or safety trial of des(1-3)IGF-I has ever been run or registered, and it has never been approved in any jurisdiction. Three things are routinely conflated and must be kept apart here: (a) IGF-1 itself, and especially rhIGF-1 / mecasermin (Increlex), which is an approved prescription drug with real human trials — none of that evidence transfers to this truncated analogue; (b) des(1-3)IGF-I’s own genuine but animal-only literature; and (c) gray-market bodybuilding claims, which are not evidence and are not scored below. Route is load-bearing: as a protein it has effectively zero oral bioavailability, so every result in the literature comes from injection or pump infusion. Its sibling analogue IGF-1 LR3 achieves IGFBP evasion by the opposite structural route — 13 residues added at the N-terminus plus an Arg³ substitution, rather than three residues removed — and is marketed as “long-acting,” though that label describes binding-protein evasion rather than any measured half-life. The two are frequently sold, conflated, and detected together.

Evidence by IndicationStrength of support · Beta

Support is an experimental score I’m building — a composite weighted by study type (human > animal > in vitro > review) and study volume. It’s a beta: a fast way to rank strength of evidence at a glance, not a validated metric. Each application links down to its write-up. Every score here is capped low for one reason: there is no human data at all. The percentages describe how well-replicated the animal evidence is; none of them describes a demonstrated human effect, and the low numbers mean “never tested in people,” not “tested and failed.”

01Anabolic & muscle-protein retention in catabolic statesShaky34%Replicated rat infusion models (diabetic, N-restricted, dexamethasone) across several labs — but contradicted in pigs and goats. No human trial.

02Gut growth & mucosal adaptationShaky32%Multiple rat gut-resection and glucocorticoid models; the compound’s most consistent in-vivo effect. Rodent only.

03Renal recovery in renal insufficiencyShaky22%Rat sub-nephrectomy plus one acute ischemic renal-failure model; largely one research group. Rat only.

04Cerebral hypoxic-ischemic neuroprotectionShaky15%A single rat intracerebroventricular study plus neuronal cell culture. Animal only, invasive route.

05”Site-specific” / localized muscle growthShaky0%Vendor and forum claim only. No study of any kind exists, in any species.

Mechanisms

Pharmacokinetics

Route is decisive. As a ~7.6 kDa protein, des(1-3)IGF-I has negligible oral bioavailability — it is digested rather than absorbed — so every in-vivo result comes from parenteral delivery: subcutaneous or intramuscular injection, or osmotic-pump infusion in the animal studies. Any oral “IGF-1 DES” product is pharmacologically inert regardless of the label.

Its defining pharmacokinetic feature is a short circulating life. In rats, plasma clearance was roughly four times faster than IGF-I (~4.6 versus ~1.2 mL/min/kg) with a larger volume of distribution, precisely because it escapes the IGFBP-3 “ternary complex” that normally keeps IGF-I parked in the bloodstream ^{3Reference 3Ballard FJ et al. · 1991AnimalPlasma clearance and tissue distribution of labelled IGF-I, IGF-II and des(1-3)IGF-I in rats — animal (rat, PK)View study →}. In lactating goats infused over 24 hours it bound only IGFBP-3, cleared faster than IGF-I, and produced a larger local mammary response ^{26Reference 26Prosser CG et al. · 1995Pharmacokinetics and bioactivity of intact versus truncated IGF-I during a 24-h infusion into lactating goats — animal (goat)View study →}. A human half-life has never been measured. This short, mostly-free profile is the whole pharmacological basis for the bodybuilding “localized action” story — the idea being that the peptide acts near the injection site before it is cleared — but that inference has never been tested for muscle growth in any species. It is detectable in human plasma and urine by high-resolution mass spectrometry at picogram-per-milliliter levels, both as an administered drug and as an endogenous IGF-I degradation product ^{11,12Reference 11Thomas A et al. · 2017Determination of LongR3-IGF-I, R3-IGF-I, Des1-3 IGF-I and their metabolites in human plasma samples by means of LC-MS — analytical (human samples, anti-doping)View study →Reference 12Mongongu C et al. · 2021Detection of LongR3-IGF-I, Des(1-3)-IGF-I and R3-IGF-I using immunopurification and high resolution mass spectrometry for antidoping purposes — analytical (anti-doping)View study →}. Gray-market material is supplied as a lyophilized powder requiring reconstitution and cold storage; stability of reconstituted product is not independently documented.

Clinical & regulatory status

Des(1-3)IGF-I has never been approved for human use in any jurisdiction and is accurately described as an unapproved research chemical. A ClinicalTrials.gov search (v2 API, July 2026) returns no trial in which des(1-3)IGF-I is the intervention — the keyword hits are unrelated pediatric-growth, GH and IGF-1-monitoring studies that merely mention IGF-1. It should not be confused with mecasermin (Increlex), recombinant full-length human IGF-1, which is an FDA-approved prescription drug for severe primary IGF-1 deficiency; that is a different molecule with a different regulatory status, and its trial evidence does not apply here.

The World Anti-Doping Agency prohibits IGF-1 and its analogues at all times under the peptide-hormones and growth-factors class of the Prohibited List, and anti-doping laboratories have built and validated dedicated mass-spectrometry assays specifically to catch des(1-3)IGF-I alongside LR3- and R3-IGF-I ^{11,12Reference 11Thomas A et al. · 2017Determination of LongR3-IGF-I, R3-IGF-I, Des1-3 IGF-I and their metabolites in human plasma samples by means of LC-MS — analytical (human samples, anti-doping)View study →Reference 12Mongongu C et al. · 2021Detection of LongR3-IGF-I, Des(1-3)-IGF-I and R3-IGF-I using immunopurification and high resolution mass spectrometry for antidoping purposes — analytical (anti-doping)View study →}. Its documented history is 1990s-onward preclinical research plus gray-market bodybuilding supply.

Last checked: July 2026.

Sourcing, Route & Legal Status

Regulatory status. des(1-3)IGF-I has never been approved as a drug or authorized as a dietary supplement anywhere, and no human clinical trial has ever tested it as a therapy. It is sold “for research use only / not for human consumption,” which is the legally accurate frame for anyone acquiring it. Marketing it for human use is unlawful in most Western jurisdictions. It is prohibited in sport at all times by WADA and is a sanctionable finding for any tested athlete. The contrast with mecasermin (rhIGF-1) is the one worth holding on to: that is full-length, prescription-controlled, pharmaceutical-grade material with an approved indication — none of which describes this compound.

How it’s supplied and administered. Sold as a lyophilized (freeze-dried) powder requiring reconstitution with bacteriostatic or sterile water, and cold storage. Because it is a protein with negligible oral bioavailability, it is used by injection — subcutaneous or intramuscular. The gray-market practice of injecting it directly into a target muscle rests on the short half-life supposedly confining its action nearby; that is an inference from rodent pharmacokinetics, not a demonstrated human effect, and it also means the dose is being placed by an untrained person using self-mixed concentrations.

Sourcing reality — this is a safety issue, not a footnote. Every commercial source is an unregulated peptide vendor: no manufacturing oversight, no pharmacopoeial identity, purity or endotoxin standard, and no assurance that the vial contains the molecule on the label rather than IGF-1, LR3, or nothing. This is not hypothetical — anti-doping analysis of black-market IGF-I-analogue products has found abundant oxidized, degraded peptide forms ^{12Reference 12Mongongu C et al. · 2021Detection of LongR3-IGF-I, Des(1-3)-IGF-I and R3-IGF-I using immunopurification and high resolution mass spectrometry for antidoping purposes — analytical (anti-doping)View study →}. Mislabeling, wrong analogue, under- or over-dosing, bacterial contamination and endotoxin are real risks, and layperson reconstitution and injection add sterility and dosing hazards on top. Third-party certificates of analysis are the minimum a buyer would need, are frequently absent or unverifiable, and can be falsified. No vendor is recommended or linked here.

Safety

There is no human safety database of any kind for des(1-3)IGF-I, so everything known comes from mechanism and animals. Greater potency at the IGF-1 receptor is at least as much a safety statement as a benefit one — the two concrete signals are hypoglycemia and tumor promotion.

Safety at a Glance

❔ Toxicity unknownDrug interactions

• Hypoglycemia is the likely dose-limiting effect. A single injected dose halved plasma glucose in mice, and escaping the binding proteins makes it worse rather than better.
• A genuine preclinical cancer signal. 53% of transgenic mice with mammary des(1-3)IGF-I expression developed adenocarcinoma by 23 months.
• Several groups sit squarely in the risk. Active or prior cancer, diabetes or any glucose-lowering therapy, pregnancy and breastfeeding, and tested athletes.
• Additive hypoglycemia with insulin and sulfonylureas. Inferred from mechanism; no interaction study exists.
• It perturbs the whole GH/IGF feedback axis. Chronic dosing in pigs reduced growth rate and food intake and depressed IGF-I, IGF-II and IGFBP-3.
• Injected gray-market product. Contamination, endotoxin exposure and dosing error from self-reconstituted concentrations.

Full Safety & Interactions Detail

Overall posture. There is no human safety database of any kind — no trial, no pharmacovigilance, no case series. Everything below is derived from mechanism, from the IGF-1-receptor-agonist class, and from preclinical findings, and each is labeled as such. Thin efficacy data does not mean a thin risk profile: this is a potent growth factor, and greater potency at the IGF-1 receptor is at least as much a safety statement as a benefit one.

• Hypoglycemia (mechanism + animal; the likely dose-limiting effect). IGF-1 has insulin-like activity, and at high doses IGF-1R agonists lower blood glucose, with weak insulin-receptor cross-activation on top. A single intraperitoneal dose of des-IGF-1 in mice reduced plasma glucose by about 50% ^{24Reference 24Li M et al. · 2002AnimalDifferential effects of des IGF-1 on Erks, Akt-1 and p70 S6K activation in mouse skeletal and cardiac muscle — animal (mouse)View study →}, and in pigs the IGFBP-evading analogues — des(1-3)IGF-I among them — were the most potent at depressing blood glucose, precisely because they bind IGFBP-3 least ^{2Reference 2Walton PE et al. · 1995AnimalIn vivo actions of IGF analogues with poor affinities for IGFBPs: metabolic and growth effects in pigs of different ages and GH responsiveness — animal (pig) reviewView study →}. Symptomatic hypoglycemia is the practical acute hazard of an injected, IGFBP-evading IGF analogue.
• Mitogenic / neoplasia concern (a real preclinical signal, not only theoretical). IGF-1R signaling is mitogenic and anti-apoptotic. In transgenic mice with mammary-targeted des(1-3)hIGF-I expression, normal apoptosis and proliferation were suppressed by ~75%, hyperplastic mammary intraepithelial lesions appeared, and 53% developed mammary adenocarcinoma by 23 months; combined with mutant p53, tumor latency was shortened by 8 months ^{15Reference 15Hadsell DL et al. · 2000AnimalCooperative interaction between mutant p53 and des(1-3)IGF-I accelerates mammary tumorigenesis — animal (transgenic mouse)View study →}. An earlier report from the same model documented incomplete mammary involution, ductile hypertrophy and loss of secretory lobules ^{14Reference 14Hadsell DL et al. · 1996AnimalTargeted expression of des(1-3) human insulin-like growth factor I in transgenic mice influences mammary gland development and IGF-binding protein expression — animal (transgenic mouse)View study →}. This is transgenic overexpression, not exogenous injection — the two are not equivalent — but it is a genuine carcinogenicity signal in the correct direction, and it is the reason the theoretical concern about promoting existing or occult tumors is taken seriously. For context, the FDA label for the approved GHRH analogue tesamorelin makes active malignancy a contraindication and requires IGF-1 monitoring on exactly this reasoning; nobody is monitoring anything here.
• A cautionary null. In a mouse myocardial ischemia-reperfusion model, intact IGF-I was cardioprotective and des-(1-3)IGF-I was not ^{13Reference 13Buerke M et al. · 1995AnimalCardioprotective effect of insulin-like growth factor I in myocardial ischemia followed by reperfusion — animal (mouse); des-(1-3)IGF-I was not cardioprotectiveView study →}. “More potent IGF” does not mean better, or safer, across tissues.
• Growth-suppression in GH-responsive species. Chronic subcutaneous dosing of IGFBP-evading analogues in pigs reduced growth rate and food intake and depressed IGF-I, IGF-II and IGFBP-3 ^{2Reference 2Walton PE et al. · 1995AnimalIn vivo actions of IGF analogues with poor affinities for IGFBPs: metabolic and growth effects in pigs of different ages and GH responsiveness — animal (pig) reviewView study →} — a reminder that this compound perturbs the whole GH/IGF feedback axis, not just one receptor.
• Interactions (mechanism-level; none assessed in humans). Plausible additive hypoglycemia with insulin, sulfonylureas and other glucose-lowering drugs. Overlapping signaling with growth hormone and GH-secretagogue peptides, which raise endogenous IGF-1 on top of an exogenous analogue. No controlled interaction study exists.
• Who should avoid it. Anyone with active or prior cancer, or meaningful cancer risk; anyone with diabetes or taking glucose-lowering therapy; anyone pregnant, breastfeeding or trying to conceive; any tested athlete; and — given the total absence of human data — effectively everyone outside a controlled research setting.
• Injection-specific risks. Injection-site reactions, non-sterile technique, contamination and endotoxin from unregulated product, and dosing error from self-reconstituted concentrations.

Scope disclosure (honesty, not a claim):

• Human data? None. No human efficacy trial, no human safety trial, no human PK study. The only human-derived data are anti-doping detection assays.
• Interactions assessed? No. Only mechanism- and class-level cautions (insulin and antidiabetics, GH/IGF-axis peptides), which are inferred rather than tested.
• Pregnancy/lactation assessed? No — not established, no reproductive-toxicity data.
• Long-term safety established? No. Absence of case reports reflects absence of study, and the transgenic-mouse tumor data actively raise a long-term concern rather than settle one.

Never imply safety from silence. Where des(1-3)IGF-I has not been studied — which is everywhere a human is involved — the correct statement is “not assessed,” not “safe.”

Pregnancy & Lactation

? Not established in pregnancy? Not established in lactation

Not assessed / not established. There are no human pregnancy or lactation data and no reproductive-toxicity study of des(1-3)IGF-I. Treat as contraindicated by default. (Preclinical note on a different molecule: the cleaved-off tripeptide GPE / (1-3)IGF-1 was ineffective and behaviorally detrimental after prenatal dosing in a 2026 rat study ^{23Reference 23Lee M et al. · 2026AnimalPrenatal (1-3)IGF-1 treatment is ineffective and behaviorally detrimental in a rat model of cortical malformation — animal (rat); concerns the GPE tripeptide, a different molecule from des(1-3)IGF-IView study →}. That is not des(1-3)IGF-I, but it underlines that manipulating the IGF axis in pregnancy is unstudied and cannot be assumed safe.)

Dosage

There is no established human dose for IGF-1 DES, and none is recommended here. Unlike most pages here, there is not even a foreign approval, a trial protocol or an off-label regimen to report as context: des(1-3)IGF-I has never been administered to a human being in a published study, so no dose has ever been shown to be safe, effective, or even tolerated. Every number circulating in bodybuilding forums and vendor copy is invented downstream of that silence.

The doses in the literature are animal doses, delivered by osmotic pump or infusion into catabolic rats, pigs and goats over days — a delivery method and a physiological context that have no bearing on a self-administered subcutaneous injection in a healthy person. They are not convertible to a human dose and are not reproduced here as one. Oral products cannot deliver intact peptide at all (see Pharmacokinetics). This entry is informational only and is not an endorsement of use.

References

1. Ballard FJ, et al. (1996). Des(1-3)IGF-I: a truncated form of insulin-like growth factor-I — review. Int J Biochem Cell Biol. https://pubmed.ncbi.nlm.nih.gov/8930132/
2. Walton PE, et al. (1995). In vivo actions of IGF analogues with poor affinities for IGFBPs: metabolic and growth effects in pigs of different ages and GH responsiveness — animal (pig) review. Prog Growth Factor Res. https://pubmed.ncbi.nlm.nih.gov/8817682/
3. Ballard FJ, et al. (1991). Plasma clearance and tissue distribution of labelled IGF-I, IGF-II and des(1-3)IGF-I in rats — animal (rat, PK). J Endocrinol. https://pubmed.ncbi.nlm.nih.gov/2005410/
4. Yamamoto H, et al. (1994). Generation of des-(1-3) insulin-like growth factor-I in serum by an acid protease — in vitro. Endocrinology. https://pubmed.ncbi.nlm.nih.gov/7988428/
5. Tomas FM, et al. (1991). Increased weight gain, nitrogen retention and muscle protein synthesis following treatment of diabetic rats with IGF-I and des(1-3)IGF-I — animal (rat). Biochem J. https://pubmed.ncbi.nlm.nih.gov/1710892/
6. Tomas FM, et al. (1993). Insulin-like growth factor-I and more potent variants restore growth of diabetic rats without inducing all characteristic insulin effects — animal (rat). Biochem J. https://pubmed.ncbi.nlm.nih.gov/7683875/
7. Tomas FM, et al. (1991). Effects of full-length and truncated insulin-like growth factor-I on nitrogen balance and muscle protein metabolism in nitrogen-restricted rats — animal (rat). J Endocrinol. https://pubmed.ncbi.nlm.nih.gov/1999680/
8. Read LC, et al. (1992). Insulin-like growth factor-I and its N-terminal modified analogues induce marked gut growth in dexamethasone-treated rats — animal (rat). J Endocrinol. https://pubmed.ncbi.nlm.nih.gov/1613443/
9. Lemmey AB, et al. (1991). IGF-I and the truncated analogue des-(1-3)IGF-I enhance growth in rats after gut resection — animal (rat). Am J Physiol. https://pubmed.ncbi.nlm.nih.gov/1996625/
10. Vanderhoof JA, et al. (1992). Truncated and native insulinlike growth factor I enhance mucosal adaptation after jejunoileal resection — animal (rat). Gastroenterology. https://pubmed.ncbi.nlm.nih.gov/1375179/
11. Thomas A, et al. (2017). Determination of LongR3-IGF-I, R3-IGF-I, Des1-3 IGF-I and their metabolites in human plasma samples by means of LC-MS — analytical (human samples, anti-doping). Growth Horm IGF Res. https://pubmed.ncbi.nlm.nih.gov/28668757/
12. Mongongu C, et al. (2021). Detection of LongR3-IGF-I, Des(1-3)-IGF-I and R3-IGF-I using immunopurification and high resolution mass spectrometry for antidoping purposes — analytical (anti-doping). Drug Test Anal. https://pubmed.ncbi.nlm.nih.gov/33587816/
13. Buerke M, et al. (1995). Cardioprotective effect of insulin-like growth factor I in myocardial ischemia followed by reperfusion — animal (mouse); des-(1-3)IGF-I was not cardioprotective. Proc Natl Acad Sci USA. https://pubmed.ncbi.nlm.nih.gov/7644533/
14. Hadsell DL, et al. (1996). Targeted expression of des(1-3) human insulin-like growth factor I in transgenic mice influences mammary gland development and IGF-binding protein expression — animal (transgenic mouse). Endocrinology. https://pubmed.ncbi.nlm.nih.gov/8536631/
15. Hadsell DL, et al. (2000). Cooperative interaction between mutant p53 and des(1-3)IGF-I accelerates mammary tumorigenesis — animal (transgenic mouse). Oncogene. https://pubmed.ncbi.nlm.nih.gov/10702797/
16. Lord AP, et al. (1994). Transfer of insulin-like growth factor-I from blood to intestine: comparison with IGFs that bind poorly to IGF-binding proteins — animal (lamb, perfused intestine). J Endocrinol. https://pubmed.ncbi.nlm.nih.gov/7520931/
17. Lemmey AB, et al. (1994). Treatment with IGF-I peptides improves function of the remnant gut following small bowel resection in rats — animal (rat). Growth Factors. https://pubmed.ncbi.nlm.nih.gov/7803042/
18. Martin AA, et al. (1991). IGF-I and its variant, des-(1-3)IGF-I, enhance growth in rats with reduced renal mass — animal (rat). Am J Physiol. https://pubmed.ncbi.nlm.nih.gov/1928375/
19. Martin AA, et al. (1992). Insulin-like growth factor I and its variant, des(1-3)IGF-I, improve nitrogen balance and food utilization in rats with renal failure — animal (rat). Miner Electrolyte Metab. https://pubmed.ncbi.nlm.nih.gov/1465072/
20. Clark R, et al. (1994). Recovery from acute ischaemic renal failure is accelerated by des-(1-3)-insulin-like growth factor-1 — animal (rat). Clin Sci (Lond). https://pubmed.ncbi.nlm.nih.gov/8062506/
21. Guan J, et al. (1996). The effects of IGF-1, IGF-2 and des-IGF-1 on neuronal loss after hypoxic-ischemic brain injury in adult rats — animal (rat). Endocrinology. https://pubmed.ncbi.nlm.nih.gov/8603600/
22. Beck KD, et al. (1993). The nature of the trophic action of BDNF, des(1-3)-insulin-like growth factor-1 and basic FGF on mesencephalic dopaminergic neurons — in vitro. Neuroscience. https://pubmed.ncbi.nlm.nih.gov/8095710/
23. Lee M, et al. (2026). Prenatal (1-3)IGF-1 treatment is ineffective and behaviorally detrimental in a rat model of cortical malformation — animal (rat); concerns the GPE tripeptide, a different molecule from des(1-3)IGF-I. Brain Behav. https://pubmed.ncbi.nlm.nih.gov/41992821/
24. Li M, et al. (2002). Differential effects of des IGF-1 on Erks, Akt-1 and p70 S6K activation in mouse skeletal and cardiac muscle — animal (mouse). Mol Cell Biochem. https://pubmed.ncbi.nlm.nih.gov/12190109/
25. Yamamoto H, et al. (1995). Enzymatic conversion of IGF-I to des(1-3)IGF-I in rat serum and tissues — animal (rat) / biochemical. J Endocrinol. https://pubmed.ncbi.nlm.nih.gov/7561610/
26. Prosser CG, et al. (1995). Pharmacokinetics and bioactivity of intact versus truncated IGF-I during a 24-h infusion into lactating goats — animal (goat). J Endocrinol. https://pubmed.ncbi.nlm.nih.gov/7891029/
27. Simes JM, et al. (1991). The effects of IGF-I, IGF-II and des(1-3)IGF-I, a potent IGF analogue, on growth hormone and IGF-binding protein secretion from cultured rat anterior pituitary cells — in vitro. J Endocrinol. https://pubmed.ncbi.nlm.nih.gov/1715381/

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