PEG-MGF

Molecular Profile

Type

PEGylated synthetic peptide (IGF-1 splice-variant E-domain, 24 residues)

Molecular weight

~2.7 kDa (unPEGylated peptide portion; approximate)

Amino acids

24

Sequence

YQPPSTNKNTKSQRRKGSTFEEHK

Modification

Covalent polyethylene-glycol conjugation of the 24-residue MGF E-peptide, intended to slow proteolysis and renal filtration of the small peptide; the PEG chain size, linker, and attachment site are not defined in primary sources. The unmodified peptide is the C-terminal E-domain of the IGF-1Ec splice variant (IGF-1Eb in rodents). Two sequence variants circulate: a synthetic analog ending …FEE-His-Lys (shown above) and the native human E-domain ending …FEE-Arg-Lys.

Mechanism & Target Class

MGF is generated by alternative splicing of the IGF-1 gene: a reading-frame shift in the E-domain-encoding exon produces a unique C-terminal E-peptide that is absent from the more abundant IGF-1Ea isoform. The mature IGF-1 region is identical across the isoforms; the isolated 24-residue E-domain peptide is the entity synthesized as MGF, and PEG-MGF is that peptide conjugated to polyethylene glycol. A defining structural feature of the isolated E-peptide is that it lacks the mature IGF-1 region present in full-length constructs: in receptor-activation bioassays the isolated 24-residue peptide produces no detectable receptor-kinase activation, in contrast to full-length constructs that retain the mature IGF-1 region. This structural distinction is the basis of the long-standing and still-contested characterization of the isolated peptide as a molecule separate from mature IGF-1. The structural rationale offered for PEGylation is that the small (~2.7 kDa) peptide is otherwise rapidly filtered and proteolyzed.

Storage & Handling

Lyophilized

-20°C; lyophilized powder typically stable months when kept desiccated and protected from light.

Handling

Small water-soluble peptide; protect from light; keep sealed and dry. Reconstitution media and exact handling are study-specific and not standardized in the primary literature.

Primary Database

PubChem CID 175675731 ↗

References (29)

1. Reviews

   1

   Zabłocka B, Goldspink PH, Goldspink G, Górecki DC. (2012). Front Endocrinol (Lausanne)

   DOI: 10.3389/fendo.2012.00131

2. 2

   Matheny RW Jr, Nindl BC, Adamo ML. (2010). Endocrinology

   DOI: 10.1210/en.2009-1217PubMed 20130113

3. 3

   Velloso CP, Harridge SDR. (2010). Scand J Med Sci Sports

   DOI: 10.1111/j.1600-0838.2009.00997.x

4. 4

   Goldspink G. (2005). Int J Biochem Cell Biol

   DOI: 10.1016/j.biocel.2005.04.006PubMed 16125110

5. 5

   Goldspink G. (2005). Physiology (Bethesda)

   DOI: 10.1152/physiol.00004.2005PubMed 16024511

6. 6

   Hill M, Wernig A, Goldspink G. (2003). J Anat

   DOI: 10.1046/j.1469-7580.2003.00195.x

7. Clinical

   7

   Philippou A, et al. (2009). In Vivo

   PubMed 19567392

8. 8

   Hameed M, et al. (2004). J Physiol

   Source

9. 9

   Hameed M, et al. (2003). J Physiol

   DOI: 10.1113/jphysiol.2002.032136PubMed 12562960

10. Primary research

    10

    medRxiv preprint. (2023). medRxiv

    DOI: 10.1101/2023.12.08.23299594

11. 11

    Mol Brain primary study. (2017). Mol Brain

    DOI: 10.1186/s13041-017-0304-0

12. 12

    Janssen JAMJL, et al. (2016). PLoS One

    DOI: 10.1371/journal.pone.0150453PubMed 26991004

13. 13

    Fornaro M, et al. (2014). Am J Physiol Endocrinol Metab

    DOI: 10.1152/ajpendo.00408.2013PubMed 24253050

14. 14

    Schlegel W, Raimann A, Halbauer D, et al. (2013). PLoS One

    DOI: 10.1371/journal.pone.0076133

15. 15

    Mavrommatis E, Shioura KM, Los T, Goldspink PH. (2013). Mol Cell Biochem

    DOI: 10.1007/s11010-013-1689-4PubMed 23712705

16. 16

    Kravchenko IV, Furalyov VA, Popov VO. (2012). Mol Cell Biochem

    DOI: 10.1007/s11010-011-1187-5

17. 17

    Esposito S, Deventer K, Van Eenoo P. (2012). Rapid Commun Mass Spectrom

    DOI: 10.1002/rcm.6144PubMed 22328223

18. 18

    Kandalla PK, Goldspink G, Butler-Browne G, Mouly V. (2011). Mech Ageing Dev

    DOI: 10.1016/j.mad.2011.02.007PubMed 21354439

19. 19

    Deng M, et al. (2011). Int Orthop

    DOI: 10.1007/s00264-010-1141-2

20. 20

    Stavropoulou A, et al. (2009). Mol Med

    DOI: 10.2119/molmed.2009.00012

21. 21

    Carpenter V, et al. (2008). Heart Lung Circ

    PubMed 17581790

22. 22

    Mills P, Dominique JC, Lafrenière JF, Bouchentouf M, Tremblay JP. (2007). Am J Transplant

    DOI: 10.1111/j.1600-6143.2007.01927.x

23. 23

    Ates K, et al. (2007). FEBS Lett

    DOI: 10.1016/j.febslet.2007.05.030PubMed 17531227

24. 24

    Dłużniewska J, et al. (2005). FASEB J

    DOI: 10.1096/fj.05-3786fjePubMed 16144956

25. 25

    Cheema U, Brown R, Mudera V, Yang SY, McGrouther G, Goldspink G. (2005). J Cell Physiol

    DOI: 10.1002/jcp.20107

26. 26

    Hill M, Goldspink G. (2003). J Physiol

    DOI: 10.1113/jphysiol.2002.035832PubMed 12692175

27. 27

    Yang SY, Goldspink G. (2002). FEBS Lett

    DOI: 10.1016/S0014-5793(02)02918-6PubMed 12095637

28. 28

    McKoy G, et al. (1999). J Physiol

    DOI: 10.1111/j.1469-7793.1999.0583v.xPubMed 10087355

29. 29

    Yang S, Alnaqeeb M, Simpson H, Goldspink G. (1996). J Muscle Res Cell Motil

    DOI: 10.1007/BF00123364PubMed 8884603