IGF-1 DES
IGF-1 DES is not a peptide. It is indexed alongside Growth factors and growth hormone-derived compounds because it appears in the same research literature and the same search demand; no statement on this site describes it as a peptide.
Identity
| Field | Value |
|---|---|
| Classification | Not a peptide |
| Primary class | Growth factors and growth hormone-derived compounds |
| CAS registry number | Unknown PubChem returned no compound record for this name on the retrieval date, so this field is not sourced. |
| PubChem CID | Unknown PubChem returned no compound record for this name on the retrieval date, so this field is not sourced. |
| UniProt accession | Unknown No UniProt query was run in v1. |
| Molecular formula | Unknown PubChem returned no compound record for this name on the retrieval date, so this field is not sourced. |
| Molecular weight | Unknown PubChem returned no compound record for this name on the retrieval date, so this field is not sourced. |
| Amino-acid sequence | Unknown Not reported by the PubChem property set retrieved for this record; no sequence database query was run in v1. |
| Reported half-life | Unknown No pharmacokinetics source was retrieved in v1. PubChem does not carry half-life as a property, so this is recorded as not yet sourced rather than estimated. |
What the cited literature examines
IGF-1 DES, reported in the literature as des(1-3)IGF-I, is insulin-like growth factor I with its first three N-terminal residues removed. It is a 67-residue protein rather than a short peptide, and PubChem returned no compound record for the name. A 1989 Biochemical Journal paper reports that IGF-binding proteins inhibit the biological activities of IGF-1 and IGF-2 but not of the des(1-3) form, and a 1995 Journal of Endocrinology paper reports enzymatic conversion of IGF-I to des(1-3)IGF-I in rat serum and tissues.
Animal records include a 1991 American Journal of Physiology paper on growth in rats after gut resection, a 2000 Oncogene paper on a cooperative interaction with mutant p53 in mammary tumorigenesis, and a 2003 Mechanisms of Ageing and Development paper on age-related differences in Akt-1 and p70 S6K activation in mouse skeletal muscle.
[2, 3, 4, 5, 6]Reported mechanism
A truncated insulin-like growth factor I whose activity, per the retrieved records, is not inhibited by IGF-binding proteins; downstream signalling through Akt-1 and p70 S6K is reported in mouse muscle.
[2, 6]Stated in the titles of the cited 1989 Biochemical Journal and 2003 Mechanisms of Ageing and Development papers.
Targets named in the cited records: IGF-1 receptor, Akt-1, p70 S6K.
FDA application register
A query of the FDA Drugs@FDA application register on 2026-10-09 returned no application records for this compound name. This compound is not approved by the FDA for human use.[1]
Scope statement: this records the result of a single automated query against the openFDA drugsfda endpoint on the stated date. It is not legal advice and is not a jurisdiction-by-jurisdiction legality assessment.
Retrieved 2026-10-09.
Amounts reported in the cited literature
Unknown. No retrieved record in this dataset states an amount, so none is shown. Where an amount is recorded it is what a named study reported administering in its own stated model, in the past tense, and is not a protocol.
No study-reported dose was taken from a source read in v1. Literature-reported values are only recorded where the retrieved citation metadata states the figure.
Adverse effects reported in the cited literature
Unknown. No retrieved record in this dataset reports an adverse effect for this compound, so no row is shown. Absence of a row records the absence of a retrieved report, nothing more.
No adverse-effect row was taken from a source read in v1. Rows are only recorded with the study model named and the reporting citation attached.
Other names
IGF-1 DES appears under these other names in the cited records or in common usage. Each one resolves to this page rather than to a separate page of its own.
- des(1-3)IGF-I
- des-IGF-1
- truncated IGF-I
Where this page sits
Research records
Cited research records for IGF-1 DES, each with its identifier, the publication type it is indexed as, and the study model stated by its assigned subject headings.
Compounds indexed next to it
- IGF-1 LR3 — Growth factors and growth hormone-derived compounds
- Mechano growth factor — Growth factors and growth hormone-derived compounds
Class page: Growth factors and growth hormone-derived compounds. Full index: all indexed compounds.
Questions this page answers
What does the cited literature examine for IGF-1 DES?
IGF-1 DES, reported in the literature as des(1-3)IGF-I, is insulin-like growth factor I with its first three N-terminal residues removed. It is a 67-residue protein rather than a short peptide, and PubChem returned no compound record for the name.
Which class is IGF-1 DES indexed under?
IGF-1 DES is indexed under Growth factors and growth hormone-derived compounds. This class groups the growth factors, growth factor fragments and growth hormone-derived proteins that research-peptide catalogues list alongside the secretagogues, most of which are proteins rather than peptides and are labelled as such on their pages.
What does the FDA application register show for IGF-1 DES?
A query of the FDA Drugs@FDA application register on 2026-10-09 returned no application records for this compound name. This compound is not approved by the FDA for human use.
Sources
- Drugs@FDA application register query for this compound, no application records returned. U.S. Food and Drug Administration, openFDA drugsfda endpoint (2026). fda:igf-1-des
- Insulin-like growth factor (IGF)-binding proteins inhibit the biological activities of IGF-1 and IGF-2 but not des-(1-3)-IGF-1. The Biochemical journal (1989). pmid:2539101
- Enzymatic conversion of IGF-I to des(1-3)IGF-I in rat serum and tissues: a further potential site of growth hormone regulation of IGF-I action. The Journal of endocrinology (1995). pmid:7561610
- IGF-I and the truncated analogue des-(1-3)IGF-I enhance growth in rats after gut resection. The American journal of physiology (1991). pmid:1996625
- Cooperative interaction between mutant p53 and des(1-3)IGF-I accelerates mammary tumorigenesis. Oncogene (2000). pmid:10702797
- Age-related differences in the des IGF-I-mediated activation of Akt-1 and p70 S6K in mouse skeletal muscle. Mechanisms of ageing and development (2003). pmid:12875741
On each stated value was matched to the record cited for it. That is record matching, not an appraisal of the research. Compiled and checked by: Peptide Monographs editorial desk. No qualified clinical reviewer.