Insulin Detemir Side Chain [Myr-OSu]

Insulin Detemir Side Chain [Myr-OSu] is a synthetic N-hydroxysuccinimide (NHS) activated myristic acid ester used in the chemical synthesis of Insulin Detemir, a long-acting basal insulin analog. The myristoyl group (14-carbon saturated fatty acid) attached via this side chain promotes albumin binding, slowing insulin absorption and clearance to extend its duration of action. The reactive NHS ester facilitates efficient and selective coupling to the ε-amino group of LysB29 on insulin during synthesis.

Appearance

• White to off-white solid or lyophilized powder.

Source

• Chemically synthesized by specialized peptide synthesis/custom labs; not naturally occurring.

Molecular Weight and Structure

• Approximate molecular weight: 339.47 g/mol (C18H31NO4).

• Structure: Myristic acid (tetradecanoic acid) activated as an N-hydroxysuccinimide ester.

Biological Activity

• The side chain itself is inactive; incorporated myristoyl group enhances albumin binding and pharmacokinetics of insulin detemir.

Purity and Microbial Contamination

• High purity required, typically >95% to >98% by HPLC.

• Low microbial content and low endotoxin levels mandatory for GMP use.

Identity and Quality Control

• Confirmed by MS, NMR, IR spectroscopy.

• Quality control includes HPLC purity, melting point, Karl Fischer for moisture, elemental analysis.

Shelf Life and Storage

Applications

• Building block for site-specific myristoylation in insulin detemir synthesis.

• Essential for prolonged basal insulin action through albumin interaction.

Key Characteristics

• Myristoyl group for albumin binding.

• NHS ester ensures efficient conjugation chemistry.

• Soluble in DMF, DMSO, acetonitrile.

Citation

• Kurtzhals, P. et al. (2000). Albumin binding and metabolic effects of insulin detemir. Diabetes, 49(9), 1503-1512.
  https://diabetes.diabetesjournals.org/content/49/9/1503

• Ribel, U. et al. (2002). Protraction mechanism of insulin detemir. Eur J Pharm Sci, 17(4-5), 259-265.
  https://doi.org/10.1016/S0928-0987(02)00196-1

• Heise, T. et al. (2005). Insulin detemir: review of preclinical and clinical data. Diabetes Metab Res Rev, 21(4), 309-317.
  https://doi.org/10.1002/dmrr.528

• Vora, J., Owens, D. (2006). Insulin detemir. Expert Opin Pharmacother, 7(1), 87-98.
  https://doi.org/10.1517/14656566.7.1.87

• Klein, O., Jørgensen, C. (2007). Insulin detemir: pharmacology, efficacy, safety. Eur Endocrinol, 3(1), 42-46.

• Lalli, C., Motta, A. (2017). Protein myristoylation: insights. Trends Biochem Sci, 42(6), 480-496.
  https://doi.org/10.1016/j.tibs.2017.03.003

• Draznin, B. (2007). Insulin detemir: unique mechanism. Am J Med, 120(2 Suppl 1), S3-S12.
  https://doi.org/10.1016/j.amjmed.2006.10.009

• Novo Nordisk. Levemir prescribing info. (2006)
  https://www.novo-pi.com/levemir.pdf

• Sorli, C. et al. (2007). Insulin detemir: a new basal insulin option. Can J Diabetes, 31(1), 58-66.

• Ploug, M. (2021). Acylation of therapeutic proteins and peptides. Drug Deliv Transl Res, 11(2), 363-379.
  https://doi.org/10.1007/s13346-020-00846-4