Chemistry:IGF-1 LR3
| Clinical data | |
|---|---|
| Other names | Long R3-IGF-1; IGF-1 Long R3 |
| Routes of administration | Injection |
| ATC code |
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| Pharmacokinetic data | |
| Elimination half-life | 56-72 hours |
| Identifiers | |
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| Chemical and physical data | |
| Formula | C400H625N111O115S9 |
| Molar mass | 9117.60 g·mol−1 |
Long arginine 3-IGF-1, abbreviated as IGF-1 LR3 or LR3-IGF-1, is a synthetic protein and lengthened analogue of human insulin-like growth factor 1 (IGF-1).[1][2] It differs from native IGF-1 in that it possesses an arginine instead of a glutamic acid at the third position in its amino acid sequence ("arginine 3"), and also has an additional 13 amino acids at its N-terminus (MFPAMPLLSLFVN) ("long"), for a total of 83 amino acids (relative to the 70 of IGF-1).[2] The consequences of these modifications are that IGF-1 LR3 retains the pharmacological activity of IGF-1 as an agonist of the IGF-1 receptor, has very low affinity for the insulin-like growth factor-binding proteins (IGFBPs), and has improved metabolic stability.[1][2] As a result, it is approximately three times more potent than IGF-1,[3] and possesses a significantly longer half-life of about 20–30 hours (relative to IGF-1's half-life of about 12–15 hours).[4]
The amino acid sequence of IGF-1 LR3 is MFPAMPLSSL FVNGPRTLCG AELVDALQFV CGDRGFYFNK PTGYGSSSRR APQTGIVDEC CFRSCDLRRL EMYCAPLKPA KSA.[5]
See also
References
- ↑ 1.0 1.1 "Superior potency of infused IGF-I analogues which bind poorly to IGF-binding proteins is maintained when administered by injection". J. Endocrinol. 150 (1): 77–84. 1996. doi:10.1677/joe.0.1500077. PMID 8708565.
- ↑ 2.0 2.1 2.2 "IGF-binding proteins are multifunctional and act via IGF-dependent and -independent mechanisms". J. Endocrinol. 175 (1): 19–31. 2002. doi:10.1677/joe.0.1750019. PMID 12379487.
- ↑ "Insulin-like growth factor-I (IGF-I) and especially IGF-I variants are anabolic in dexamethasone-treated rats". Biochem. J. 282 ( Pt 1) (Pt 1): 91–7. 1992. doi:10.1042/bj2820091. PMID 1371669.
- ↑ "IGF-1 has plaque-stabilizing effects in atherosclerosis by altering vascular smooth muscle cell phenotype". Am. J. Pathol. 178 (2): 924–34. 2011. doi:10.1016/j.ajpath.2010.10.007. PMID 21281823.
- ↑ Mario Thevis (13 December 2010). Mass Spectrometry in Sports Drug Testing: Characterization of Prohibited Substances and Doping Control Analytical Assays. John Wiley & Sons. pp. 252–. ISBN 978-1-118-03514-6. https://books.google.com/books?id=dWHQMev5mHwC&pg=PA252.
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